D-enantiomers of 15-residue cecropin A-melittin hybrids.
Identifieur interne : 002B10 ( PubMed/Checkpoint ); précédent : 002B09; suivant : 002B11D-enantiomers of 15-residue cecropin A-melittin hybrids.
Auteurs : E L Merrifield [États-Unis] ; S A Mitchell ; J. Ubach ; H G Boman ; D. Andreu ; R B MerrifieldSource :
- International journal of peptide and protein research [ 0367-8377 ]
Descripteurs français
- KwdFr :
- Antibactériens (), Bactéries à Gram négatif (), Bactéries à Gram positif (), Conductivité électrique, Conformation des protéines, Dichroïsme circulaire, Fragments peptidiques (), Hormones des insectes (), Multimérisation de protéines, Mélittine (), Peptides (), Peptides antimicrobiens cationiques, Spectrophotométrie, Stabilité de médicament, Stéréoisomérie, Trypsine.
- MESH :
- Antibactériens, Bactéries à Gram négatif, Bactéries à Gram positif, Conductivité électrique, Conformation des protéines, Dichroïsme circulaire, Fragments peptidiques, Hormones des insectes, Multimérisation de protéines, Mélittine, Peptides, Peptides antimicrobiens cationiques, Spectrophotométrie, Stabilité de médicament, Stéréoisomérie, Trypsine.
English descriptors
- KwdEn :
- Anti-Bacterial Agents (chemistry), Antimicrobial Cationic Peptides, Circular Dichroism, Drug Stability, Electric Conductivity, Gram-Negative Bacteria (drug effects), Gram-Positive Bacteria (drug effects), Insect Hormones (chemistry), Melitten (chemistry), Peptide Fragments (chemistry), Peptides (chemistry), Protein Conformation, Protein Multimerization, Spectrophotometry, Stereoisomerism, Trypsin.
- MESH :
- chemical , chemistry : Anti-Bacterial Agents, Insect Hormones, Melitten, Peptide Fragments, Peptides.
- chemical : Antimicrobial Cationic Peptides, Trypsin.
- drug effects : Gram-Negative Bacteria, Gram-Positive Bacteria.
- Circular Dichroism, Drug Stability, Electric Conductivity, Protein Conformation, Protein Multimerization, Spectrophotometry, Stereoisomerism.
Abstract
The all-D enantiomers of six 15-residue hybrids of cecropin A and melittin were synthesized. They contained the seven N-terminal residues of cecropin A, followed by eight residues from the N-terminal region of melittin. They were pure and of the correct composition and structure. The peptides were compared with their all-L enantiomers. The L and D isomer pairs were each exact mirror images by circular dichroism at several concentrations of hexafluoroisopropanol, and at 12 or 20% were highly helical. The L analogs were rapidly hydrolyzed by trypsin but the D analogs were very resistant, making them suitable candidates for orally active drugs. These 15-mers did not form ion channels in normal lipid bilayers made in decane, but those bilayers made in squalene were thinner and the peptides did form ion-conducting channels. The D/L pairs of peptides were very active antibiotics against five representative Gram-negative and Gram-positive bacteria. In each case the D and L isomers were essentially equally active within experimental error. This is interpreted to mean that the peptides do not act by tight interactions with chiral receptors, enzymes or lipids. The action of these peptides against these organisms is best explained by self-aggregation and the formation of ion-conducting pores across bacterial membranes.
DOI: 10.1111/j.1399-3011.1995.tb00592.x
PubMed: 8537174
Affiliations:
Links toward previous steps (curation, corpus...)
Links to Exploration step
pubmed:8537174Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">D-enantiomers of 15-residue cecropin A-melittin hybrids.</title><author><name sortKey="Merrifield, E L" sort="Merrifield, E L" uniqKey="Merrifield E" first="E L" last="Merrifield">E L Merrifield</name><affiliation wicri:level="2"><nlm:affiliation>Rockefeller University, New York, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Rockefeller University, New York</wicri:regionArea><placeName><region type="state">État de New York</region></placeName></affiliation></author><author><name sortKey="Mitchell, S A" sort="Mitchell, S A" uniqKey="Mitchell S" first="S A" last="Mitchell">S A Mitchell</name></author><author><name sortKey="Ubach, J" sort="Ubach, J" uniqKey="Ubach J" first="J" last="Ubach">J. Ubach</name></author><author><name sortKey="Boman, H G" sort="Boman, H G" uniqKey="Boman H" first="H G" last="Boman">H G Boman</name></author><author><name sortKey="Andreu, D" sort="Andreu, D" uniqKey="Andreu D" first="D" last="Andreu">D. Andreu</name></author><author><name sortKey="Merrifield, R B" sort="Merrifield, R B" uniqKey="Merrifield R" first="R B" last="Merrifield">R B Merrifield</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="????"><PubDate><MedlineDate>1995 Sep-Oct</MedlineDate></PubDate></date><idno type="RBID">pubmed:8537174</idno><idno type="pmid">8537174</idno><idno type="doi">10.1111/j.1399-3011.1995.tb00592.x</idno><idno type="wicri:Area/PubMed/Corpus">002807</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002807</idno><idno type="wicri:Area/PubMed/Curation">002807</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002807</idno><idno type="wicri:Area/PubMed/Checkpoint">002B10</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002B10</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">D-enantiomers of 15-residue cecropin A-melittin hybrids.</title><author><name sortKey="Merrifield, E L" sort="Merrifield, E L" uniqKey="Merrifield E" first="E L" last="Merrifield">E L Merrifield</name><affiliation wicri:level="2"><nlm:affiliation>Rockefeller University, New York, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Rockefeller University, New York</wicri:regionArea><placeName><region type="state">État de New York</region></placeName></affiliation></author><author><name sortKey="Mitchell, S A" sort="Mitchell, S A" uniqKey="Mitchell S" first="S A" last="Mitchell">S A Mitchell</name></author><author><name sortKey="Ubach, J" sort="Ubach, J" uniqKey="Ubach J" first="J" last="Ubach">J. Ubach</name></author><author><name sortKey="Boman, H G" sort="Boman, H G" uniqKey="Boman H" first="H G" last="Boman">H G Boman</name></author><author><name sortKey="Andreu, D" sort="Andreu, D" uniqKey="Andreu D" first="D" last="Andreu">D. Andreu</name></author><author><name sortKey="Merrifield, R B" sort="Merrifield, R B" uniqKey="Merrifield R" first="R B" last="Merrifield">R B Merrifield</name></author></analytic><series><title level="j">International journal of peptide and protein research</title><idno type="ISSN">0367-8377</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Anti-Bacterial Agents (chemistry)</term><term>Antimicrobial Cationic Peptides</term><term>Circular Dichroism</term><term>Drug Stability</term><term>Electric Conductivity</term><term>Gram-Negative Bacteria (drug effects)</term><term>Gram-Positive Bacteria (drug effects)</term><term>Insect Hormones (chemistry)</term><term>Melitten (chemistry)</term><term>Peptide Fragments (chemistry)</term><term>Peptides (chemistry)</term><term>Protein Conformation</term><term>Protein Multimerization</term><term>Spectrophotometry</term><term>Stereoisomerism</term><term>Trypsin</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antibactériens ()</term><term>Bactéries à Gram négatif ()</term><term>Bactéries à Gram positif ()</term><term>Conductivité électrique</term><term>Conformation des protéines</term><term>Dichroïsme circulaire</term><term>Fragments peptidiques ()</term><term>Hormones des insectes ()</term><term>Multimérisation de protéines</term><term>Mélittine ()</term><term>Peptides ()</term><term>Peptides antimicrobiens cationiques</term><term>Spectrophotométrie</term><term>Stabilité de médicament</term><term>Stéréoisomérie</term><term>Trypsine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Anti-Bacterial Agents</term><term>Insect Hormones</term><term>Melitten</term><term>Peptide Fragments</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Antimicrobial Cationic Peptides</term><term>Trypsin</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Gram-Negative Bacteria</term><term>Gram-Positive Bacteria</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Circular Dichroism</term><term>Drug Stability</term><term>Electric Conductivity</term><term>Protein Conformation</term><term>Protein Multimerization</term><term>Spectrophotometry</term><term>Stereoisomerism</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Antibactériens</term><term>Bactéries à Gram négatif</term><term>Bactéries à Gram positif</term><term>Conductivité électrique</term><term>Conformation des protéines</term><term>Dichroïsme circulaire</term><term>Fragments peptidiques</term><term>Hormones des insectes</term><term>Multimérisation de protéines</term><term>Mélittine</term><term>Peptides</term><term>Peptides antimicrobiens cationiques</term><term>Spectrophotométrie</term><term>Stabilité de médicament</term><term>Stéréoisomérie</term><term>Trypsine</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The all-D enantiomers of six 15-residue hybrids of cecropin A and melittin were synthesized. They contained the seven N-terminal residues of cecropin A, followed by eight residues from the N-terminal region of melittin. They were pure and of the correct composition and structure. The peptides were compared with their all-L enantiomers. The L and D isomer pairs were each exact mirror images by circular dichroism at several concentrations of hexafluoroisopropanol, and at 12 or 20% were highly helical. The L analogs were rapidly hydrolyzed by trypsin but the D analogs were very resistant, making them suitable candidates for orally active drugs. These 15-mers did not form ion channels in normal lipid bilayers made in decane, but those bilayers made in squalene were thinner and the peptides did form ion-conducting channels. The D/L pairs of peptides were very active antibiotics against five representative Gram-negative and Gram-positive bacteria. In each case the D and L isomers were essentially equally active within experimental error. This is interpreted to mean that the peptides do not act by tight interactions with chiral receptors, enzymes or lipids. The action of these peptides against these organisms is best explained by self-aggregation and the formation of ion-conducting pores across bacterial membranes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8537174</PMID><DateCompleted><Year>1996</Year><Month>02</Month><Day>08</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>05</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0367-8377</ISSN><JournalIssue CitedMedium="Print"><Volume>46</Volume><Issue>3-4</Issue><PubDate><MedlineDate>1995 Sep-Oct</MedlineDate></PubDate></JournalIssue><Title>International journal of peptide and protein research</Title><ISOAbbreviation>Int. J. Pept. Protein Res.</ISOAbbreviation></Journal><ArticleTitle>D-enantiomers of 15-residue cecropin A-melittin hybrids.</ArticleTitle><Pagination><MedlinePgn>214-20</MedlinePgn></Pagination><Abstract><AbstractText>The all-D enantiomers of six 15-residue hybrids of cecropin A and melittin were synthesized. They contained the seven N-terminal residues of cecropin A, followed by eight residues from the N-terminal region of melittin. They were pure and of the correct composition and structure. The peptides were compared with their all-L enantiomers. The L and D isomer pairs were each exact mirror images by circular dichroism at several concentrations of hexafluoroisopropanol, and at 12 or 20% were highly helical. The L analogs were rapidly hydrolyzed by trypsin but the D analogs were very resistant, making them suitable candidates for orally active drugs. These 15-mers did not form ion channels in normal lipid bilayers made in decane, but those bilayers made in squalene were thinner and the peptides did form ion-conducting channels. The D/L pairs of peptides were very active antibiotics against five representative Gram-negative and Gram-positive bacteria. In each case the D and L isomers were essentially equally active within experimental error. This is interpreted to mean that the peptides do not act by tight interactions with chiral receptors, enzymes or lipids. The action of these peptides against these organisms is best explained by self-aggregation and the formation of ion-conducting pores across bacterial membranes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Merrifield</LastName><ForeName>E L</ForeName><Initials>EL</Initials><AffiliationInfo><Affiliation>Rockefeller University, New York, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mitchell</LastName><ForeName>S A</ForeName><Initials>SA</Initials></Author><Author ValidYN="Y"><LastName>Ubach</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Boman</LastName><ForeName>H G</ForeName><Initials>HG</Initials></Author><Author ValidYN="Y"><LastName>Andreu</LastName><ForeName>D</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Merrifield</LastName><ForeName>R B</ForeName><Initials>RB</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>DK01260</GrantID><Acronym>DK</Acronym><Agency>NIDDK NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Denmark</Country><MedlineTA>Int J Pept Protein Res</MedlineTA><NlmUniqueID>0330420</NlmUniqueID><ISSNLinking>0367-8377</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000900">Anti-Bacterial Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D023181">Antimicrobial Cationic Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007301">Insect Hormones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010446">Peptide Fragments</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>20449-79-0</RegistryNumber><NameOfSubstance UI="D008555">Melitten</NameOfSubstance></Chemical><Chemical><RegistryNumber>80451-04-3</RegistryNumber><NameOfSubstance UI="C031161">cecropin A</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.4</RegistryNumber><NameOfSubstance UI="D014357">Trypsin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000900" MajorTopicYN="N">Anti-Bacterial Agents</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D023181" MajorTopicYN="Y">Antimicrobial Cationic Peptides</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004355" MajorTopicYN="N">Drug Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004553" MajorTopicYN="N">Electric Conductivity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006090" MajorTopicYN="N">Gram-Negative Bacteria</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006094" MajorTopicYN="N">Gram-Positive Bacteria</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007301" MajorTopicYN="N">Insect Hormones</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008555" MajorTopicYN="N">Melitten</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010446" MajorTopicYN="N">Peptide Fragments</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013053" MajorTopicYN="N">Spectrophotometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013237" MajorTopicYN="N">Stereoisomerism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014357" MajorTopicYN="N">Trypsin</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1995</Year><Month>9</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1995</Year><Month>9</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1995</Year><Month>9</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8537174</ArticleId><ArticleId IdType="doi">10.1111/j.1399-3011.1995.tb00592.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>État de New York</li></region></list><tree><noCountry><name sortKey="Andreu, D" sort="Andreu, D" uniqKey="Andreu D" first="D" last="Andreu">D. Andreu</name><name sortKey="Boman, H G" sort="Boman, H G" uniqKey="Boman H" first="H G" last="Boman">H G Boman</name><name sortKey="Merrifield, R B" sort="Merrifield, R B" uniqKey="Merrifield R" first="R B" last="Merrifield">R B Merrifield</name><name sortKey="Mitchell, S A" sort="Mitchell, S A" uniqKey="Mitchell S" first="S A" last="Mitchell">S A Mitchell</name><name sortKey="Ubach, J" sort="Ubach, J" uniqKey="Ubach J" first="J" last="Ubach">J. Ubach</name></noCountry><country name="États-Unis"><region name="État de New York"><name sortKey="Merrifield, E L" sort="Merrifield, E L" uniqKey="Merrifield E" first="E L" last="Merrifield">E L Merrifield</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/PubMed/Checkpoint
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002B10 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd -nk 002B10 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= PubMed
|étape= Checkpoint
|type= RBID
|clé= pubmed:8537174
|texte= D-enantiomers of 15-residue cecropin A-melittin hybrids.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Checkpoint/RBID.i -Sk "pubmed:8537174" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Checkpoint/biblio.hfd \
| NlmPubMed2Wicri -a MersV1
| This area was generated with Dilib version V0.6.33. |  |