Conformational investigation of α,β‐dehydropeptides VII. Conformation of Ac‐Pro‐ΔAla‐NHCH3 and Ac‐Pro‐(E)‐ΔAbu‐NHCH3: comparison with (Z)‐substituted α,β‐dehydropeptides†
Identifieur interne : 001561 ( Istex/Corpus ); précédent : 001560; suivant : 001562Conformational investigation of α,β‐dehydropeptides VII. Conformation of Ac‐Pro‐ΔAla‐NHCH3 and Ac‐Pro‐(E)‐ΔAbu‐NHCH3: comparison with (Z)‐substituted α,β‐dehydropeptides†
Auteurs : C. Pietrzy Aski ; B. Rzeszotarska ; E. Ciszak ; M. Lisowski ; Z. Kubica ; G. BoussardSource :
- International Journal of Peptide and Protein Research [ 0367-8377 ] ; 1996-10.
English descriptors
- KwdEn :
- Aala, Aala residue, Absorption spectra, Amino acid, Axaa, Axaa aala, Bioactive peptides, Cdci, Chem, Chemical shifts, Conformation, Conformational, Conformational freedom, Conformational propensities, Conformer, Crystal structure, Dehydroalanine, Dehydroalanine residue, Ethyl ether, Isobutyl chlorocarbonate, Kubica, Minor conformer, Model peptides, Molecular conformation, Nhch, Pepride protein, Peptide, Peptide bonds, Peptide protein, Pietrzynski, Previous work, Proline residue, Proton, Resonance linewidths, Rzeszotarska, Solution conformation, Solvent dependencies, Trans, Trans isomer, Unit cell, Various solvents.
- Teeft :
- Aala, Aala residue, Absorption spectra, Amino acid, Axaa, Axaa aala, Bioactive peptides, Cdci, Chem, Chemical shifts, Conformation, Conformational, Conformational freedom, Conformational propensities, Conformer, Crystal structure, Dehydroalanine, Dehydroalanine residue, Ethyl ether, Isobutyl chlorocarbonate, Kubica, Minor conformer, Model peptides, Molecular conformation, Nhch, Pepride protein, Peptide, Peptide bonds, Peptide protein, Pietrzynski, Previous work, Proline residue, Proton, Resonance linewidths, Rzeszotarska, Solution conformation, Solvent dependencies, Trans, Trans isomer, Unit cell, Various solvents.
Abstract
The crystal structure and solution conformation of Ac‐Pro‐ΔAla‐NHCH3 and the solution conformation of Ac‐Pro‐(E)‐ΔAbu‐NHCH3 were investigated by X‐ray diffraction method and NMR, FTIR and CD spectroscopies. Ac‐Pro‐ΔAla‐NHCH, adopts an extended‐coil conformation in the crystalline state, with all‐trans peptide bonds and the ΔAla residue being in a C5 form, φ1=– 71.4(4), ψ1=– 16.8(4), φ2=– 178.4(3) and ψ2= 172.4(3)°. In inert solvents the peptide also assumes the C5 conformation, but a γ‐turn on the Pro residue cannot be ruled out. In these solvents Ac‐Pro‐(E)‐ ΔAbu‐NHCH3 accommodates a βII‐turn, but a minor conformer with a nearly planar disposition of the CO—NH and C=C bonds (φ2∼0°) is also present. Previous spectroscopic studies of the (Z)‐substituted dehydropeptides Ac‐Pro‐(Z)‐ ΔAbu‐NHCH, and Ac‐Pro‐ΔVal‐NHCH3 reveal that both peptides prefer a βII‐turn in solution. Comparison of conformations in the family of four Ac‐Pro‐ΔXaa‐NHCH3 peptides let us formulate the following order of their tendency to adopt a β‐turn in solution: (Z)‐ ΔAbu > (E)‐ δAbu > ΔVal; ΔAla does not. None of the folded structures formed by the four compounds is stable in strongly solvating media. © Munksgaard 1996.
Url:
DOI: 10.1111/j.1399-3011.1996.tb00851.x
Links to Exploration step
ISTEX:88F750669484C93CBC90291C09CAD5C7BD15AF2CLe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Conformational investigation of α,β‐dehydropeptides VII. Conformation of Ac‐Pro‐ΔAla‐NHCH3 and Ac‐Pro‐(E)‐ΔAbu‐NHCH3: comparison with (Z)‐substituted α,β‐dehydropeptides†</title><author><name sortKey="Pietrzy Aski, C" sort="Pietrzy Aski, C" uniqKey="Pietrzy Aski C" first="C." last="Pietrzy Aski">C. Pietrzy Aski</name><affiliation><mods:affiliation>Department of Organic Chemistry, University of Opole, Opole, Poland</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: gp@uni.opole. pl</mods:affiliation></affiliation></author><author><name sortKey="Rzeszotarska, B" sort="Rzeszotarska, B" uniqKey="Rzeszotarska B" first="B." last="Rzeszotarska">B. Rzeszotarska</name><affiliation><mods:affiliation>Department of Organic Chemistry, University of Opole, Opole, Poland</mods:affiliation></affiliation></author><author><name sortKey="Ciszak, E" sort="Ciszak, E" uniqKey="Ciszak E" first="E." last="Ciszak">E. Ciszak</name><affiliation><mods:affiliation>Hauptman‐Woodward Medical Research Institute, Buffalo, New York, USA</mods:affiliation></affiliation></author><author><name sortKey="Lisowski, M" sort="Lisowski, M" uniqKey="Lisowski M" first="M." last="Lisowski">M. Lisowski</name><affiliation><mods:affiliation>Institute of Chemistry, University of Wroclaw, Wroclaw, Poland</mods:affiliation></affiliation></author><author><name sortKey="Kubica, Z" sort="Kubica, Z" uniqKey="Kubica Z" first="Z." last="Kubica">Z. Kubica</name><affiliation><mods:affiliation>Department of Organic Chemistry, University of Opole, Opole, Poland</mods:affiliation></affiliation></author><author><name sortKey="Boussard, G" sort="Boussard, G" uniqKey="Boussard G" first="G." last="Boussard">G. Boussard</name><affiliation><mods:affiliation>CNRS‐ URA‐494, ENSIC‐INPL, Nancy, France</mods:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:88F750669484C93CBC90291C09CAD5C7BD15AF2C</idno><date when="1996" year="1996">1996</date><idno type="doi">10.1111/j.1399-3011.1996.tb00851.x</idno><idno type="url">https://api.istex.fr/document/88F750669484C93CBC90291C09CAD5C7BD15AF2C/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001561</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001561</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main">Conformational investigation of α,β‐dehydropeptides VII<ref type="note" target="#fn1">*</ref>. Conformation of Ac‐Pro‐ΔAla‐NHCH<hi rend="subscript">3</hi> and Ac‐Pro‐(<hi rend="italic">E</hi>)‐ΔAbu‐NHCH<hi rend="subscript">3</hi>: comparison with (<hi rend="italic">Z</hi>)‐substituted α,β‐dehydropeptides†</title><author><name sortKey="Pietrzy Aski, C" sort="Pietrzy Aski, C" uniqKey="Pietrzy Aski C" first="C." last="Pietrzy Aski">C. Pietrzy Aski</name><affiliation><mods:affiliation>Department of Organic Chemistry, University of Opole, Opole, Poland</mods:affiliation></affiliation><affiliation><mods:affiliation>E-mail: gp@uni.opole. pl</mods:affiliation></affiliation></author><author><name sortKey="Rzeszotarska, B" sort="Rzeszotarska, B" uniqKey="Rzeszotarska B" first="B." last="Rzeszotarska">B. Rzeszotarska</name><affiliation><mods:affiliation>Department of Organic Chemistry, University of Opole, Opole, Poland</mods:affiliation></affiliation></author><author><name sortKey="Ciszak, E" sort="Ciszak, E" uniqKey="Ciszak E" first="E." last="Ciszak">E. Ciszak</name><affiliation><mods:affiliation>Hauptman‐Woodward Medical Research Institute, Buffalo, New York, USA</mods:affiliation></affiliation></author><author><name sortKey="Lisowski, M" sort="Lisowski, M" uniqKey="Lisowski M" first="M." last="Lisowski">M. Lisowski</name><affiliation><mods:affiliation>Institute of Chemistry, University of Wroclaw, Wroclaw, Poland</mods:affiliation></affiliation></author><author><name sortKey="Kubica, Z" sort="Kubica, Z" uniqKey="Kubica Z" first="Z." last="Kubica">Z. Kubica</name><affiliation><mods:affiliation>Department of Organic Chemistry, University of Opole, Opole, Poland</mods:affiliation></affiliation></author><author><name sortKey="Boussard, G" sort="Boussard, G" uniqKey="Boussard G" first="G." last="Boussard">G. Boussard</name><affiliation><mods:affiliation>CNRS‐ URA‐494, ENSIC‐INPL, Nancy, France</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">International Journal of Peptide and Protein Research</title><title level="j" type="alt">INTERNATIONAL JOURNAL OF PEPTIDE AND PROTEIN RESEARCH</title><idno type="ISSN">0367-8377</idno><idno type="eISSN">1399-3011</idno><imprint><biblScope unit="vol">48</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="347">347</biblScope><biblScope unit="page" to="356">356</biblScope><biblScope unit="page-count">10</biblScope><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1996-10">1996-10</date></imprint><idno type="ISSN">0367-8377</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0367-8377</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aala</term><term>Aala residue</term><term>Absorption spectra</term><term>Amino acid</term><term>Axaa</term><term>Axaa aala</term><term>Bioactive peptides</term><term>Cdci</term><term>Chem</term><term>Chemical shifts</term><term>Conformation</term><term>Conformational</term><term>Conformational freedom</term><term>Conformational propensities</term><term>Conformer</term><term>Crystal structure</term><term>Dehydroalanine</term><term>Dehydroalanine residue</term><term>Ethyl ether</term><term>Isobutyl chlorocarbonate</term><term>Kubica</term><term>Minor conformer</term><term>Model peptides</term><term>Molecular conformation</term><term>Nhch</term><term>Pepride protein</term><term>Peptide</term><term>Peptide bonds</term><term>Peptide protein</term><term>Pietrzynski</term><term>Previous work</term><term>Proline residue</term><term>Proton</term><term>Resonance linewidths</term><term>Rzeszotarska</term><term>Solution conformation</term><term>Solvent dependencies</term><term>Trans</term><term>Trans isomer</term><term>Unit cell</term><term>Various solvents</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Aala</term><term>Aala residue</term><term>Absorption spectra</term><term>Amino acid</term><term>Axaa</term><term>Axaa aala</term><term>Bioactive peptides</term><term>Cdci</term><term>Chem</term><term>Chemical shifts</term><term>Conformation</term><term>Conformational</term><term>Conformational freedom</term><term>Conformational propensities</term><term>Conformer</term><term>Crystal structure</term><term>Dehydroalanine</term><term>Dehydroalanine residue</term><term>Ethyl ether</term><term>Isobutyl chlorocarbonate</term><term>Kubica</term><term>Minor conformer</term><term>Model peptides</term><term>Molecular conformation</term><term>Nhch</term><term>Pepride protein</term><term>Peptide</term><term>Peptide bonds</term><term>Peptide protein</term><term>Pietrzynski</term><term>Previous work</term><term>Proline residue</term><term>Proton</term><term>Resonance linewidths</term><term>Rzeszotarska</term><term>Solution conformation</term><term>Solvent dependencies</term><term>Trans</term><term>Trans isomer</term><term>Unit cell</term><term>Various solvents</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The crystal structure and solution conformation of Ac‐Pro‐ΔAla‐NHCH3 and the solution conformation of Ac‐Pro‐(E)‐ΔAbu‐NHCH3 were investigated by X‐ray diffraction method and NMR, FTIR and CD spectroscopies. Ac‐Pro‐ΔAla‐NHCH, adopts an extended‐coil conformation in the crystalline state, with all‐trans peptide bonds and the ΔAla residue being in a C5 form, φ1=– 71.4(4), ψ1=– 16.8(4), φ2=– 178.4(3) and ψ2= 172.4(3)°. In inert solvents the peptide also assumes the C5 conformation, but a γ‐turn on the Pro residue cannot be ruled out. In these solvents Ac‐Pro‐(E)‐ ΔAbu‐NHCH3 accommodates a βII‐turn, but a minor conformer with a nearly planar disposition of the CO—NH and C=C bonds (φ2∼0°) is also present. Previous spectroscopic studies of the (Z)‐substituted dehydropeptides Ac‐Pro‐(Z)‐ ΔAbu‐NHCH, and Ac‐Pro‐ΔVal‐NHCH3 reveal that both peptides prefer a βII‐turn in solution. Comparison of conformations in the family of four Ac‐Pro‐ΔXaa‐NHCH3 peptides let us formulate the following order of their tendency to adopt a β‐turn in solution: (Z)‐ ΔAbu > (E)‐ δAbu > ΔVal; ΔAla does not. None of the folded structures formed by the four compounds is stable in strongly solvating media. © Munksgaard 1996.</div></front></TEI><istex><corpusName>wiley</corpusName><keywords><teeft><json:string>peptide</json:string><json:string>nhch</json:string><json:string>rzeszotarska</json:string><json:string>chem</json:string><json:string>aala</json:string><json:string>pietrzynski</json:string><json:string>dehydroalanine</json:string><json:string>trans</json:string><json:string>peptide protein</json:string><json:string>cdci</json:string><json:string>conformation</json:string><json:string>conformer</json:string><json:string>axaa</json:string><json:string>kubica</json:string><json:string>dehydroalanine residue</json:string><json:string>solution conformation</json:string><json:string>crystal structure</json:string><json:string>chemical shifts</json:string><json:string>aala residue</json:string><json:string>peptide bonds</json:string><json:string>various solvents</json:string><json:string>resonance linewidths</json:string><json:string>conformational freedom</json:string><json:string>previous work</json:string><json:string>molecular conformation</json:string><json:string>proline residue</json:string><json:string>minor conformer</json:string><json:string>conformational propensities</json:string><json:string>unit cell</json:string><json:string>model peptides</json:string><json:string>pepride protein</json:string><json:string>amino acid</json:string><json:string>ethyl ether</json:string><json:string>trans isomer</json:string><json:string>axaa aala</json:string><json:string>bioactive peptides</json:string><json:string>absorption spectra</json:string><json:string>solvent dependencies</json:string><json:string>isobutyl chlorocarbonate</json:string><json:string>conformational</json:string><json:string>proton</json:string></teeft></keywords><author><json:item><name>C. PIETRZYŃASKI</name><affiliations><json:string>Department of Organic Chemistry, University of Opole, Opole, Poland</json:string><json:string>E-mail: gp@uni.opole. pl</json:string></affiliations></json:item><json:item><name>B. RZESZOTARSKA</name><affiliations><json:string>Department of Organic Chemistry, University of Opole, Opole, Poland</json:string></affiliations></json:item><json:item><name>E. CISZAK</name><affiliations><json:string>Hauptman‐Woodward Medical Research Institute, Buffalo, New York, USA</json:string></affiliations></json:item><json:item><name>M. LISOWSKI</name><affiliations><json:string>Institute of Chemistry, University of Wroclaw, Wroclaw, Poland</json:string></affiliations></json:item><json:item><name>Z. KUBICA</name><affiliations><json:string>Department of Organic Chemistry, University of Opole, Opole, Poland</json:string></affiliations></json:item><json:item><name>G. BOUSSARD</name><affiliations><json:string>CNRS‐ URA‐494, ENSIC‐INPL, Nancy, France</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>circular dichroism</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>C5 conformation</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>crystal structure</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>dehydroalanine</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>β‐dehydrobutyrine</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>β‐dehydropeptide conformation</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>infrared spectroscopy</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>nuclear magnetic resonance</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>β‐turn</value></json:item></subject><articleId><json:string>CBDD347</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>The crystal structure and solution conformation of Ac‐Pro‐ΔAla‐NHCH3 and the solution conformation of Ac‐Pro‐(E)‐ΔAbu‐NHCH3 were investigated by X‐ray diffraction method and NMR, FTIR and CD spectroscopies. Ac‐Pro‐ΔAla‐NHCH, adopts an extended‐coil conformation in the crystalline state, with all‐trans peptide bonds and the ΔAla residue being in a C5 form, φ1=– 71.4(4), ψ1=– 16.8(4), φ2=– 178.4(3) and ψ2= 172.4(3)°. In inert solvents the peptide also assumes the C5 conformation, but a γ‐turn on the Pro residue cannot be ruled out. In these solvents Ac‐Pro‐(E)‐ ΔAbu‐NHCH3 accommodates a βII‐turn, but a minor conformer with a nearly planar disposition of the CO—NH and C=C bonds (φ2∼0°) is also present. Previous spectroscopic studies of the (Z)‐substituted dehydropeptides Ac‐Pro‐(Z)‐ ΔAbu‐NHCH, and Ac‐Pro‐ΔVal‐NHCH3 reveal that both peptides prefer a βII‐turn in solution. Comparison of conformations in the family of four Ac‐Pro‐ΔXaa‐NHCH3 peptides let us formulate the following order of their tendency to adopt a β‐turn in solution: (Z)‐ ΔAbu > (E)‐ δAbu > ΔVal; ΔAla does not. None of the folded structures formed by the four compounds is stable in strongly solvating media. © Munksgaard 1996.</abstract><qualityIndicators><score>7.648</score><pdfVersion>1.4</pdfVersion><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><abstractCharCount>1205</abstractCharCount><pdfWordCount>5028</pdfWordCount><pdfCharCount>30716</pdfCharCount><pdfPageCount>10</pdfPageCount><abstractWordCount>179</abstractWordCount></qualityIndicators><title>Conformational investigation of α,β‐dehydropeptides VII. Conformation of Ac‐Pro‐ΔAla‐NHCH3 and Ac‐Pro‐(E)‐ΔAbu‐NHCH3: comparison with (Z)‐substituted α,β‐dehydropeptides†</title><genre><json:string>article</json:string></genre><host><title>International Journal of Peptide and Protein Research</title><language><json:string>unknown</json:string></language><doi><json:string>10.1111/(ISSN)1399-3011a</json:string></doi><issn><json:string>0367-8377</json:string></issn><eissn><json:string>1399-3011</json:string></eissn><publisherId><json:string>CBDD</json:string></publisherId><volume>48</volume><issue>4</issue><pages><first>347</first><last>356</last><total>10</total></pages><genre><json:string>journal</json:string></genre></host><categories><inist><json:string>sciences appliquees, technologies et medecines</json:string><json:string>sciences biologiques et medicales</json:string><json:string>sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1996</publicationDate><copyrightDate>1996</copyrightDate><doi><json:string>10.1111/j.1399-3011.1996.tb00851.x</json:string></doi><id>88F750669484C93CBC90291C09CAD5C7BD15AF2C</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/88F750669484C93CBC90291C09CAD5C7BD15AF2C/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/88F750669484C93CBC90291C09CAD5C7BD15AF2C/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/88F750669484C93CBC90291C09CAD5C7BD15AF2C/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main">Conformational investigation of α,β‐dehydropeptides VII<ref type="note" target="#fn1">*</ref>. Conformation of Ac‐Pro‐ΔAla‐NHCH<hi rend="subscript">3</hi> and Ac‐Pro‐(<hi rend="italic">E</hi>)‐ΔAbu‐NHCH<hi rend="subscript">3</hi>: comparison with (<hi rend="italic">Z</hi>)‐substituted α,β‐dehydropeptides†</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1996-10"></date></publicationStmt><notesStmt><note type="content-type" subtype="article" source="article" scheme="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</note><note type="publication-type" subtype="journal" scheme="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</note></notesStmt><sourceDesc><biblStruct type="article"><analytic><title level="a" type="main">Conformational investigation of α,β‐dehydropeptides VII<ref type="note" target="#fn1">*</ref>. Conformation of Ac‐Pro‐ΔAla‐NHCH<hi rend="subscript">3</hi> and Ac‐Pro‐(<hi rend="italic">E</hi>)‐ΔAbu‐NHCH<hi rend="subscript">3</hi>: comparison with (<hi rend="italic">Z</hi>)‐substituted α,β‐dehydropeptides†</title><author xml:id="author-0000" role="corresp"><persName><forename type="first">C.</forename><surname>PIETRZYŃASKI</surname></persName><affiliation>Department of Organic Chemistry, University of Opole, Opole, Poland<address><country key="PL"></country></address></affiliation><affiliation>Address: Dr. Grzegorz Pietrzynáski Department of Organic Chemistry University of Opole ul. Oleska 48 45–052 Opole Poland Fax: (+ 4877)538387 E‐mail: gp@uni.opole. pl</affiliation></author><author xml:id="author-0001"><persName><forename type="first">B.</forename><surname>RZESZOTARSKA</surname></persName><affiliation>Department of Organic Chemistry, University of Opole, Opole, Poland<address><country key="PL"></country></address></affiliation></author><author xml:id="author-0002"><persName><forename type="first">E.</forename><surname>CISZAK</surname></persName><affiliation>Hauptman‐Woodward Medical Research Institute, Buffalo, New York, USA<address><country key="US"></country></address></affiliation></author><author xml:id="author-0003"><persName><forename type="first">M.</forename><surname>LISOWSKI</surname></persName><affiliation>Institute of Chemistry, University of Wroclaw, Wroclaw, Poland<address><country key="PL"></country></address></affiliation></author><author xml:id="author-0004"><persName><forename type="first">Z.</forename><surname>KUBICA</surname></persName><affiliation>Department of Organic Chemistry, University of Opole, Opole, Poland<address><country key="PL"></country></address></affiliation></author><author xml:id="author-0005"><persName><forename type="first">G.</forename><surname>BOUSSARD</surname></persName><affiliation>CNRS‐ URA‐494, ENSIC‐INPL, Nancy, France<address><country key="FR"></country></address></affiliation></author><idno type="istex">88F750669484C93CBC90291C09CAD5C7BD15AF2C</idno><idno type="ark">ark:/67375/WNG-2MSBZQ84-7</idno><idno type="DOI">10.1111/j.1399-3011.1996.tb00851.x</idno><idno type="unit">CBDD347</idno><idno type="toTypesetVersion">file:CBDD.CBDD347.pdf</idno></analytic><monogr><title level="j" type="main">International Journal of Peptide and Protein Research</title><title level="j" type="alt">INTERNATIONAL JOURNAL OF PEPTIDE AND PROTEIN RESEARCH</title><idno type="pISSN">0367-8377</idno><idno type="eISSN">1399-3011</idno><idno type="book-DOI">10.1111/(ISSN)1399-3011a</idno><idno type="book-part-DOI">10.1111/jpp.1996.48.issue-4</idno><idno type="product">CBDD</idno><idno type="publisherDivision">ST</idno><imprint><biblScope unit="vol">48</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="347">347</biblScope><biblScope unit="page" to="356">356</biblScope><biblScope unit="page-count">10</biblScope><publisher>Blackwell Publishing Ltd</publisher><pubPlace>Oxford, UK</pubPlace><date type="published" when="1996-10"></date></imprint></monogr></biblStruct></sourceDesc></fileDesc><profileDesc><abstract xml:lang="en" style="main"><p>The crystal structure and solution conformation of Ac‐Pro‐ΔAla‐NHCH<hi rend="subscript">3</hi> and the solution conformation of Ac‐Pro‐(<hi rend="italic">E</hi>)‐ΔAbu‐NHCH<hi rend="subscript">3</hi> were investigated by X‐ray diffraction method and NMR, FTIR and CD spectroscopies. Ac‐Pro‐ΔAla‐NHCH, adopts an extended‐coil conformation in the crystalline state, with <hi rend="italic">all‐trans</hi> peptide bonds and the ΔAla residue being in a C<hi rend="subscript">5</hi> form, φ<hi rend="subscript">1</hi>=– 71.4(4), ψ<hi rend="subscript">1</hi>=– 16.8(4), φ<hi rend="subscript">2</hi>=– 178.4(3) and ψ<hi rend="subscript">2</hi>= 172.4(3)°. In inert solvents the peptide also assumes the C<hi rend="subscript">5</hi> conformation, but a γ‐turn on the Pro residue cannot be ruled out. In these solvents Ac‐Pro‐(<hi rend="italic">E</hi>)‐ ΔAbu‐NHCH<hi rend="subscript">3</hi> accommodates a βII‐turn, but a minor conformer with a nearly planar disposition of the CO—NH and C=C bonds (φ<hi rend="subscript">2</hi>∼0°) is also present. Previous spectroscopic studies of the (Z)‐substituted dehydropeptides Ac‐Pro‐(<hi rend="italic">Z</hi>)‐ ΔAbu‐NHCH, and Ac‐Pro‐ΔVal‐NHCH<hi rend="subscript">3</hi> reveal that both peptides prefer a βII‐turn in solution. Comparison of conformations in the family of four Ac‐Pro‐ΔXaa‐NHCH<hi rend="subscript">3</hi> peptides let us formulate the following order of their tendency to adopt a β‐turn in solution: (<hi rend="italic">Z</hi>)‐ ΔAbu > (E)‐ δAbu > ΔVal; ΔAla does not. None of the folded structures formed by the four compounds is stable in strongly solvating media. © Munksgaard 1996.</p></abstract><textClass><keywords xml:lang="en"><term xml:id="k1">circular dichroism</term><term xml:id="k2">C<hi rend="subscript">5</hi> conformation</term><term xml:id="k3">crystal structure</term><term xml:id="k4">dehydroalanine</term><term xml:id="k6">β‐dehydrobutyrine</term><term xml:id="k8">β‐dehydropeptide conformation</term><term xml:id="k9">infrared spectroscopy</term><term xml:id="k10">nuclear magnetic resonance</term><term xml:id="k11">β‐turn</term></keywords></textClass><langUsage><language ident="en"></language></langUsage></profileDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/88F750669484C93CBC90291C09CAD5C7BD15AF2C/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>Blackwell Publishing Ltd</publisherName><publisherLoc>Oxford, UK</publisherLoc></publisherInfo><doi origin="wiley" registered="yes">10.1111/(ISSN)1399-3011a</doi><issn type="print">0367-8377</issn><issn type="electronic">1399-3011</issn><idGroup><id type="product" value="CBDD"></id><id type="publisherDivision" value="ST"></id></idGroup><titleGroup><title type="main" sort="INTERNATIONAL JOURNAL OF PEPTIDE AND PROTEIN RESEARCH">International Journal of Peptide and Protein Research</title></titleGroup></publicationMeta><publicationMeta level="part" position="10004"><doi origin="wiley">10.1111/jpp.1996.48.issue-4</doi><numberingGroup><numbering type="journalVolume" number="48">48</numbering><numbering type="journalIssue" number="4">4</numbering></numberingGroup><coverDate startDate="1996-10">October 1996</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="0034700" status="forIssue"><doi origin="wiley">10.1111/j.1399-3011.1996.tb00851.x</doi><idGroup><id type="unit" value="CBDD347"></id></idGroup><countGroup><count type="pageTotal" number="10"></count></countGroup><eventGroup><event type="firstOnline" date="2009-01-12"></event><event type="publishedOnlineFinalForm" date="2009-01-12"></event><event type="xmlConverted" agent="Converter:BPG_TO_WML3G version:2.3.5 mode:FullText source:HeaderRef result:HeaderRef" date="2010-04-07"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-08"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-23"></event></eventGroup><numberingGroup><numbering type="pageFirst" number="347">347</numbering><numbering type="pageLast" number="356">356</numbering></numberingGroup><correspondenceTo>Address: Dr. <i>Grzegorz Pietrzynáski</i> Department of Organic Chemistry University of Opole ul. Oleska 48 45–052 Opole Poland Fax: (+ 4877)538387 E‐mail: <email normalForm="gp@uni.opole. pl">gp@uni.opole. pl</email></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:CBDD.CBDD347.pdf"></link></linkGroup></publicationMeta><contentMeta><unparsedEditorialHistory>Received 11 October 1995, revised 17 January, accepted for publication 6 May 1996</unparsedEditorialHistory><countGroup><count type="referenceTotal" number="56"></count><count type="linksCrossRef" number="8"></count></countGroup><titleGroup><title type="main">Conformational investigation of α,β‐dehydropeptides VII<link href="#fn1">*</link>. Conformation of Ac‐Pro‐ΔAla‐NHCH<sub>3</sub> and Ac‐Pro‐(<i>E</i>)‐ΔAbu‐NHCH<sub>3</sub>: comparison with (<i>Z</i>)‐substituted α,β‐dehydropeptides†</title></titleGroup><creators><creator creatorRole="author" xml:id="cr1" affiliationRef="#a1" corresponding="yes"><personName><givenNames>C.</givenNames><familyName>PIETRZYŃASKI</familyName></personName></creator><creator creatorRole="author" xml:id="cr2" affiliationRef="#a1"><personName><givenNames>B.</givenNames><familyName>RZESZOTARSKA</familyName></personName></creator><creator creatorRole="author" xml:id="cr3" affiliationRef="#a2"><personName><givenNames>E.</givenNames><familyName>CISZAK</familyName></personName></creator><creator creatorRole="author" xml:id="cr4" affiliationRef="#a3"><personName><givenNames>M.</givenNames><familyName>LISOWSKI</familyName></personName></creator><creator creatorRole="author" xml:id="cr5" affiliationRef="#a1"><personName><givenNames>Z.</givenNames><familyName>KUBICA</familyName></personName></creator><creator creatorRole="author" xml:id="cr6" affiliationRef="#a4"><personName><givenNames>G.</givenNames><familyName>BOUSSARD</familyName></personName></creator></creators><affiliationGroup><affiliation xml:id="a1" countryCode="PL"><unparsedAffiliation>Department of Organic Chemistry, University of Opole, Opole, Poland</unparsedAffiliation></affiliation><affiliation xml:id="a2" countryCode="US"><unparsedAffiliation>Hauptman‐Woodward Medical Research Institute, Buffalo, New York, USA</unparsedAffiliation></affiliation><affiliation xml:id="a3" countryCode="PL"><unparsedAffiliation>Institute of Chemistry, University of Wroclaw, Wroclaw, Poland</unparsedAffiliation></affiliation><affiliation xml:id="a4" countryCode="FR"><unparsedAffiliation>CNRS‐ URA‐494, ENSIC‐INPL, Nancy, France</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en"><keyword xml:id="k1">circular dichroism</keyword><keyword xml:id="k2">C<sub>5</sub> conformation</keyword><keyword xml:id="k3">crystal structure</keyword><keyword xml:id="k4">dehydroalanine</keyword><keyword xml:id="k6">β‐dehydrobutyrine</keyword><keyword xml:id="k8">β‐dehydropeptide conformation</keyword><keyword xml:id="k9">infrared spectroscopy</keyword><keyword xml:id="k10">nuclear magnetic resonance</keyword><keyword xml:id="k11">β‐turn</keyword></keywordGroup><abstractGroup><abstract type="main" xml:lang="en"><p>The crystal structure and solution conformation of Ac‐Pro‐ΔAla‐NHCH<sub>3</sub> and the solution conformation of Ac‐Pro‐(<i>E</i>)‐ΔAbu‐NHCH<sub>3</sub> were investigated by X‐ray diffraction method and NMR, FTIR and CD spectroscopies. Ac‐Pro‐ΔAla‐NHCH, adopts an extended‐coil conformation in the crystalline state, with <i>all‐trans</i> peptide bonds and the ΔAla residue being in a C<sub>5</sub> form, φ<sub>1</sub>=– 71.4(4), ψ<sub>1</sub>=– 16.8(4), φ<sub>2</sub>=– 178.4(3) and ψ<sub>2</sub>= 172.4(3)°. In inert solvents the peptide also assumes the C<sub>5</sub> conformation, but a γ‐turn on the Pro residue cannot be ruled out. In these solvents Ac‐Pro‐(<i>E</i>)‐ ΔAbu‐NHCH<sub>3</sub> accommodates a βII‐turn, but a minor conformer with a nearly planar disposition of the CO—NH and C=C bonds (φ<sub>2</sub>∼0°) is also present. Previous spectroscopic studies of the (Z)‐substituted dehydropeptides Ac‐Pro‐(<i>Z</i>)‐ ΔAbu‐NHCH, and Ac‐Pro‐ΔVal‐NHCH<sub>3</sub> reveal that both peptides prefer a βII‐turn in solution. Comparison of conformations in the family of four Ac‐Pro‐ΔXaa‐NHCH<sub>3</sub> peptides let us formulate the following order of their tendency to adopt a β‐turn in solution: (<i>Z</i>)‐ ΔAbu > (E)‐ δAbu > ΔVal; ΔAla does not. None of the folded structures formed by the four compounds is stable in strongly solvating media. © Munksgaard 1996.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="fn1"><label>*</label><p>For Part VI of this series see ref. 1.</p></note></noteGroup></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Conformational investigation of α,β‐dehydropeptides VII. Conformation of Ac‐Pro‐ΔAla‐NHCH3 and Ac‐Pro‐(E)‐ΔAbu‐NHCH3: comparison with (Z)‐substituted α,β‐dehydropeptides†</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Conformational investigation of α,β‐dehydropeptides VII*. Conformation of Ac‐Pro‐ΔAla‐NHCH3 and Ac‐Pro‐(E)‐ΔAbu‐NHCH3: comparison with (Z)‐substituted α,β‐dehydropeptides†</title></titleInfo><name type="personal"><namePart type="given">C.</namePart><namePart type="family">PIETRZYŃASKI</namePart><affiliation>Department of Organic Chemistry, University of Opole, Opole, Poland</affiliation><affiliation>E-mail: gp@uni.opole. pl</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">B.</namePart><namePart type="family">RZESZOTARSKA</namePart><affiliation>Department of Organic Chemistry, University of Opole, Opole, Poland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">E.</namePart><namePart type="family">CISZAK</namePart><affiliation>Hauptman‐Woodward Medical Research Institute, Buffalo, New York, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">M.</namePart><namePart type="family">LISOWSKI</namePart><affiliation>Institute of Chemistry, University of Wroclaw, Wroclaw, Poland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Z.</namePart><namePart type="family">KUBICA</namePart><affiliation>Department of Organic Chemistry, University of Opole, Opole, Poland</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">G.</namePart><namePart type="family">BOUSSARD</namePart><affiliation>CNRS‐ URA‐494, ENSIC‐INPL, Nancy, France</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><place><placeTerm type="text">Oxford, UK</placeTerm></place><dateIssued encoding="w3cdtf">1996-10</dateIssued><edition>Received 11 October 1995, revised 17 January, accepted for publication 6 May 1996</edition><copyrightDate encoding="w3cdtf">1996</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><extent unit="references">56</extent><extent unit="linksCrossRef">8</extent></physicalDescription><abstract lang="en">The crystal structure and solution conformation of Ac‐Pro‐ΔAla‐NHCH3 and the solution conformation of Ac‐Pro‐(E)‐ΔAbu‐NHCH3 were investigated by X‐ray diffraction method and NMR, FTIR and CD spectroscopies. Ac‐Pro‐ΔAla‐NHCH, adopts an extended‐coil conformation in the crystalline state, with all‐trans peptide bonds and the ΔAla residue being in a C5 form, φ1=– 71.4(4), ψ1=– 16.8(4), φ2=– 178.4(3) and ψ2= 172.4(3)°. In inert solvents the peptide also assumes the C5 conformation, but a γ‐turn on the Pro residue cannot be ruled out. In these solvents Ac‐Pro‐(E)‐ ΔAbu‐NHCH3 accommodates a βII‐turn, but a minor conformer with a nearly planar disposition of the CO—NH and C=C bonds (φ2∼0°) is also present. Previous spectroscopic studies of the (Z)‐substituted dehydropeptides Ac‐Pro‐(Z)‐ ΔAbu‐NHCH, and Ac‐Pro‐ΔVal‐NHCH3 reveal that both peptides prefer a βII‐turn in solution. Comparison of conformations in the family of four Ac‐Pro‐ΔXaa‐NHCH3 peptides let us formulate the following order of their tendency to adopt a β‐turn in solution: (Z)‐ ΔAbu > (E)‐ δAbu > ΔVal; ΔAla does not. None of the folded structures formed by the four compounds is stable in strongly solvating media. © Munksgaard 1996.</abstract><note type="content">*For Part VI of this series see ref. 1.</note><subject lang="en"><genre>keywords</genre><topic>circular dichroism</topic><topic>C5 conformation</topic><topic>crystal structure</topic><topic>dehydroalanine</topic><topic>β‐dehydrobutyrine</topic><topic>β‐dehydropeptide conformation</topic><topic>infrared spectroscopy</topic><topic>nuclear magnetic resonance</topic><topic>β‐turn</topic></subject><relatedItem type="host"><titleInfo><title>International Journal of Peptide and Protein Research</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><identifier type="ISSN">0367-8377</identifier><identifier type="eISSN">1399-3011</identifier><identifier type="DOI">10.1111/(ISSN)1399-3011a</identifier><identifier type="PublisherID">CBDD</identifier><part><date>1996</date><detail type="volume"><caption>vol.</caption><number>48</number></detail><detail type="issue"><caption>no.</caption><number>4</number></detail><extent unit="pages"><start>347</start><end>356</end><total>10</total></extent></part></relatedItem><identifier type="istex">88F750669484C93CBC90291C09CAD5C7BD15AF2C</identifier><identifier type="ark">ark:/67375/WNG-2MSBZQ84-7</identifier><identifier type="DOI">10.1111/j.1399-3011.1996.tb00851.x</identifier><identifier type="ArticleID">CBDD347</identifier><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-L0C46X92-X">wiley</recordContentSource><recordOrigin>Blackwell Publishing Ltd</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/document/88F750669484C93CBC90291C09CAD5C7BD15AF2C/metadata/json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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