NMR study on a SRYD-containing fibronectin-like sequence (250–257) of Leishmania gp63: contribution of residual water in the dimethyl sulfoxide solution structure
Identifieur interne : 000E66 ( Istex/Checkpoint ); précédent : 000E65; suivant : 000E67NMR study on a SRYD-containing fibronectin-like sequence (250–257) of Leishmania gp63: contribution of residual water in the dimethyl sulfoxide solution structure
Auteurs : Vassilias Tsikaris ; Mahn Thong Cung ; Constantinos Sakarellos ; Athina K. Tzinia ; Ketty P. Soterladou ; Maria Sakarellos-DaitsiotisSource :
- Journal of the Chemical Society, Perkin Transactions 2 [ 0300-9580 ] ; 1994.
English descriptors
- KwdEn :
- Amide, Chem, Coefficient, Conformational, Connectivity, Data points, Diagonal peaks, Dmso, Dmso peptide solution, Dmso solution, Hohaha, Hohaha experiment, Hydrate, Iasrydql octapeptide, Molecular sieves, Octapeptide, Octapeptide hydrate, Peptide, Peptide hydrate, Perkin, Perkin trans, Possible interaction, Proton, Residual, Residual water, Resonance data, Roesy, Roesy spectrum, Same sign, Sieve, Synthetic octapeptide, Temperature coefficient, Temperature coefficient values, Trace water, Trans.
- Teeft :
- Amide, Chem, Coefficient, Conformational, Connectivity, Data points, Diagonal peaks, Dmso, Dmso peptide solution, Dmso solution, Hohaha, Hohaha experiment, Hydrate, Iasrydql octapeptide, Molecular sieves, Octapeptide, Octapeptide hydrate, Peptide, Peptide hydrate, Perkin, Perkin trans, Possible interaction, Proton, Residual, Residual water, Resonance data, Roesy, Roesy spectrum, Same sign, Sieve, Synthetic octapeptide, Temperature coefficient, Temperature coefficient values, Trace water, Trans.
Abstract
The conformational characteristics of the I250ASRYDQL257 synthetic octapeptide, which incorporates the SRYD adhesion site (252–255) of Leishmania gp63, have been investigated at pH 2 and 5, by means of 1 D and 2D 1H NMR spectroscopy (temperature coefficient values, chemical shifts, vicinal coupling constants and NOE effects). It was found that elimination of residual water from the dimethyl sulfoxide (DMSO) solution at pH 2 provides exchange peaks in the ROESY and HOHAHA spectra similar to those obtained for the DMSO peptide solution at pH 5. This common structure is stabilized (i) by the formation of a type I β-turn involving the QNH→RCO interaction and (ii) by a possible interaction between the guanidinium and the D-β-carboxylate groups. After treatment with molecular sieves, the remaining residual water is redistributed between the peptide functional groups and participates in the rigidification of the new conformational state.
Url:
DOI: 10.1039/P29940000821
Affiliations:
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Tzinia</name></author><author wicri:is="90%"><name sortKey="Soterladou, Ketty P" sort="Soterladou, Ketty P" uniqKey="Soterladou K" first="Ketty P." last="Soterladou">Ketty P. Soterladou</name></author><author wicri:is="90%"><name sortKey="Sakarellos Daitsiotis, Maria" sort="Sakarellos Daitsiotis, Maria" uniqKey="Sakarellos Daitsiotis M" first="Maria" last="Sakarellos-Daitsiotis">Maria Sakarellos-Daitsiotis</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:C65D4067551148C7555E7DE99EB1B955AAA96923</idno><date when="1994" year="1994">1994</date><idno type="doi">10.1039/P29940000821</idno><idno type="url">https://api.istex.fr/document/C65D4067551148C7555E7DE99EB1B955AAA96923/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001833</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001833</idno><idno type="wicri:Area/Istex/Curation">001833</idno><idno type="wicri:Area/Istex/Checkpoint">000E66</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">000E66</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a">NMR study on a SRYD-containing fibronectin-like sequence (250–257) of Leishmania gp63: contribution of residual water in the dimethyl sulfoxide solution structure</title><author wicri:is="90%"><name sortKey="Tsikaris, Vassilias" sort="Tsikaris, Vassilias" uniqKey="Tsikaris V" first="Vassilias" last="Tsikaris">Vassilias Tsikaris</name></author><author wicri:is="90%"><name sortKey="Cung, Mahn Thong" sort="Cung, Mahn Thong" uniqKey="Cung M" first="Mahn Thong" last="Cung">Mahn Thong Cung</name></author><author wicri:is="90%"><name sortKey="Sakarellos, Constantinos" sort="Sakarellos, Constantinos" uniqKey="Sakarellos C" first="Constantinos" last="Sakarellos">Constantinos Sakarellos</name></author><author wicri:is="90%"><name sortKey="Tzinia, Athina K" sort="Tzinia, Athina K" uniqKey="Tzinia A" first="Athina K." last="Tzinia">Athina K. Tzinia</name></author><author wicri:is="90%"><name sortKey="Soterladou, Ketty P" sort="Soterladou, Ketty P" uniqKey="Soterladou K" first="Ketty P." last="Soterladou">Ketty P. Soterladou</name></author><author wicri:is="90%"><name sortKey="Sakarellos Daitsiotis, Maria" sort="Sakarellos Daitsiotis, Maria" uniqKey="Sakarellos Daitsiotis M" first="Maria" last="Sakarellos-Daitsiotis">Maria Sakarellos-Daitsiotis</name></author></analytic><monogr></monogr><series><title level="j">Journal of the Chemical Society, Perkin Transactions 2</title><title level="j" type="abbrev">J. Chem. Soc., Perkin Trans. 2</title><idno type="ISSN">0300-9580</idno><idno type="eISSN">1364-5471</idno><imprint><publisher>The Royal Society of Chemistry.</publisher><date type="published" when="1994">1994</date><biblScope unit="volume">0</biblScope><biblScope unit="issue">4</biblScope><biblScope unit="page" from="821">821</biblScope><biblScope unit="page" to="826">826</biblScope></imprint><idno type="ISSN">0300-9580</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0300-9580</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amide</term><term>Chem</term><term>Coefficient</term><term>Conformational</term><term>Connectivity</term><term>Data points</term><term>Diagonal peaks</term><term>Dmso</term><term>Dmso peptide solution</term><term>Dmso solution</term><term>Hohaha</term><term>Hohaha experiment</term><term>Hydrate</term><term>Iasrydql octapeptide</term><term>Molecular sieves</term><term>Octapeptide</term><term>Octapeptide hydrate</term><term>Peptide</term><term>Peptide hydrate</term><term>Perkin</term><term>Perkin trans</term><term>Possible interaction</term><term>Proton</term><term>Residual</term><term>Residual water</term><term>Resonance data</term><term>Roesy</term><term>Roesy spectrum</term><term>Same sign</term><term>Sieve</term><term>Synthetic octapeptide</term><term>Temperature coefficient</term><term>Temperature coefficient values</term><term>Trace water</term><term>Trans</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Amide</term><term>Chem</term><term>Coefficient</term><term>Conformational</term><term>Connectivity</term><term>Data points</term><term>Diagonal peaks</term><term>Dmso</term><term>Dmso peptide solution</term><term>Dmso solution</term><term>Hohaha</term><term>Hohaha experiment</term><term>Hydrate</term><term>Iasrydql octapeptide</term><term>Molecular sieves</term><term>Octapeptide</term><term>Octapeptide hydrate</term><term>Peptide</term><term>Peptide hydrate</term><term>Perkin</term><term>Perkin trans</term><term>Possible interaction</term><term>Proton</term><term>Residual</term><term>Residual water</term><term>Resonance data</term><term>Roesy</term><term>Roesy spectrum</term><term>Same sign</term><term>Sieve</term><term>Synthetic octapeptide</term><term>Temperature coefficient</term><term>Temperature coefficient values</term><term>Trace water</term><term>Trans</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract">The conformational characteristics of the I250ASRYDQL257 synthetic octapeptide, which incorporates the SRYD adhesion site (252–255) of Leishmania gp63, have been investigated at pH 2 and 5, by means of 1 D and 2D 1H NMR spectroscopy (temperature coefficient values, chemical shifts, vicinal coupling constants and NOE effects). It was found that elimination of residual water from the dimethyl sulfoxide (DMSO) solution at pH 2 provides exchange peaks in the ROESY and HOHAHA spectra similar to those obtained for the DMSO peptide solution at pH 5. This common structure is stabilized (i) by the formation of a type I β-turn involving the QNH→RCO interaction and (ii) by a possible interaction between the guanidinium and the D-β-carboxylate groups. After treatment with molecular sieves, the remaining residual water is redistributed between the peptide functional groups and participates in the rigidification of the new conformational state.</div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Cung, Mahn Thong" sort="Cung, Mahn Thong" uniqKey="Cung M" first="Mahn Thong" last="Cung">Mahn Thong Cung</name><name sortKey="Sakarellos Daitsiotis, Maria" sort="Sakarellos Daitsiotis, Maria" uniqKey="Sakarellos Daitsiotis M" first="Maria" last="Sakarellos-Daitsiotis">Maria Sakarellos-Daitsiotis</name><name sortKey="Sakarellos, Constantinos" sort="Sakarellos, Constantinos" uniqKey="Sakarellos C" first="Constantinos" last="Sakarellos">Constantinos Sakarellos</name><name sortKey="Soterladou, Ketty P" sort="Soterladou, Ketty P" uniqKey="Soterladou K" first="Ketty P." last="Soterladou">Ketty P. Soterladou</name><name sortKey="Tsikaris, Vassilias" sort="Tsikaris, Vassilias" uniqKey="Tsikaris V" first="Vassilias" last="Tsikaris">Vassilias Tsikaris</name><name sortKey="Tzinia, Athina K" sort="Tzinia, Athina K" uniqKey="Tzinia A" first="Athina K." last="Tzinia">Athina K. Tzinia</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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