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Article: Effect of side chains on turns and helices in peptides of β 3-aminoxy acids

TitleEffect of side chains on turns and helices in peptides of β 3-aminoxy acids
Authors
Issue Date2004
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.html
Citation
Journal Of The American Chemical Society, 2004, v. 126 n. 22, p. 6956-6966 How to Cite?
AbstractWe have investigated, using NMR, IR, and CD spectroscopy and X-ray crystallography, the conformational properties of peptides 1-10 of β 3-aminoxy acids (NH 2OCHRCH 2COOH) having different side chains on the β carbon atom (e.g., R = Me, Et, COOBn, CH 2CH 2CH=CH 2, i-Bu, i-Pr). The β N-O turns and β N-O helices that involve a nine-membered-ring intramolecular hydrogen bond between NH 1+2 and CO 1, which have been found previously in peptides β 2,2-aminoxy acids (NH 2OCH 2CMe 2COOH), are also present in those β 3-aminoxy peptides. X-ray crystal structures and NMR spectral analysis reveal that, in the β N-O turns and β N-O helices induced by β 3-aminoxy acids, the N-O bond could be either anti or gauche to the C α-C β bond depending on the size of the side chain; in contrast, only the anti conformation was found in β 2,2-aminoxy peptides. Both diamide 1 and triamide 9 exist in different conformations in solution and in the solid state: parallel sheet structures in the solid state and predominantly β N-O turn and β N-O helix conformations in nonpolar solvents. Theoretical studies on a series of model diamides rationalize very well the experimentally observed conformational features of these β 3-aminoxy peptides.
Persistent Identifierhttp://hdl.handle.net/10722/167990
ISSN
2015 Impact Factor: 13.038
2015 SCImago Journal Rankings: 7.123
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorYang, Den_HK
dc.contributor.authorZhang, YHen_HK
dc.contributor.authorLi, Ben_HK
dc.contributor.authorZhang, DWen_HK
dc.contributor.authorChan, JCYen_HK
dc.contributor.authorZhu, NYen_HK
dc.contributor.authorLuo, SWen_HK
dc.contributor.authorWu, YDen_HK
dc.date.accessioned2012-10-08T03:13:50Z-
dc.date.available2012-10-08T03:13:50Z-
dc.date.issued2004en_HK
dc.identifier.citationJournal Of The American Chemical Society, 2004, v. 126 n. 22, p. 6956-6966en_HK
dc.identifier.issn0002-7863en_HK
dc.identifier.urihttp://hdl.handle.net/10722/167990-
dc.description.abstractWe have investigated, using NMR, IR, and CD spectroscopy and X-ray crystallography, the conformational properties of peptides 1-10 of β 3-aminoxy acids (NH 2OCHRCH 2COOH) having different side chains on the β carbon atom (e.g., R = Me, Et, COOBn, CH 2CH 2CH=CH 2, i-Bu, i-Pr). The β N-O turns and β N-O helices that involve a nine-membered-ring intramolecular hydrogen bond between NH 1+2 and CO 1, which have been found previously in peptides β 2,2-aminoxy acids (NH 2OCH 2CMe 2COOH), are also present in those β 3-aminoxy peptides. X-ray crystal structures and NMR spectral analysis reveal that, in the β N-O turns and β N-O helices induced by β 3-aminoxy acids, the N-O bond could be either anti or gauche to the C α-C β bond depending on the size of the side chain; in contrast, only the anti conformation was found in β 2,2-aminoxy peptides. Both diamide 1 and triamide 9 exist in different conformations in solution and in the solid state: parallel sheet structures in the solid state and predominantly β N-O turn and β N-O helix conformations in nonpolar solvents. Theoretical studies on a series of model diamides rationalize very well the experimentally observed conformational features of these β 3-aminoxy peptides.en_HK
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/journals/jacsat/index.htmlen_HK
dc.relation.ispartofJournal of the American Chemical Societyen_HK
dc.subject.meshAcids - Chemistryen_US
dc.subject.meshAminationen_US
dc.subject.meshCircular Dichroismen_US
dc.subject.meshCrystallography, X-Rayen_US
dc.subject.meshMagnetic Resonance Spectroscopyen_US
dc.subject.meshMolecular Structureen_US
dc.subject.meshPeptides - Chemistryen_US
dc.subject.meshProtein Structure, Secondaryen_US
dc.titleEffect of side chains on turns and helices in peptides of β 3-aminoxy acidsen_HK
dc.typeArticleen_HK
dc.identifier.emailYang, D: yangdan@hku.hken_HK
dc.identifier.emailZhu, NY: nzhu@hkucc.hku.hken_HK
dc.identifier.authorityYang, D=rp00825en_HK
dc.identifier.authorityZhu, NY=rp00845en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1021/ja049976sen_HK
dc.identifier.pmid15174865-
dc.identifier.scopuseid_2-s2.0-3042777861en_HK
dc.identifier.hkuros94547-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-3042777861&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume126en_HK
dc.identifier.issue22en_HK
dc.identifier.spage6956en_HK
dc.identifier.epage6966en_HK
dc.identifier.isiWOS:000221828200034-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridYang, D=7404800756en_HK
dc.identifier.scopusauthoridZhang, YH=8379010100en_HK
dc.identifier.scopusauthoridLi, B=36072052100en_HK
dc.identifier.scopusauthoridZhang, DW=35320759400en_HK
dc.identifier.scopusauthoridChan, JCY=55230705500en_HK
dc.identifier.scopusauthoridZhu, NY=7201449530en_HK
dc.identifier.scopusauthoridLuo, SW=35741176500en_HK
dc.identifier.scopusauthoridWu, YD=7406892738en_HK

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