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Article: Chiral α-aminoxy acid/achiral cyclopropane α-aminoxy acid unit as a building block for constructing the α N-O helix

TitleChiral α-aminoxy acid/achiral cyclopropane α-aminoxy acid unit as a building block for constructing the α N-O helix
Authors
Issue Date2010
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/joc
Citation
Journal Of Organic Chemistry, 2010, v. 75 n. 14, p. 4796-4805 How to Cite?
Abstract
(Figure Presented) The monomer 1 derived from achiral 1-(aminoxy) cyclopropanecarboxylic acid (OAcc) and oligopeptides 2-9 consisting of a chiral α-aminoxy acid and an achiral α-aminoxy acid such as OAcc were synthesized and their structures characterized. The eight-membered-ring intramolecular hydrogen bond, namely the α N-O turn, was formed between adjacent residues independent of their chirality. However, the helix formation was sequence-dependent. Dipeptide 2 bearing chiral α-aminoxy acid (d-OAA) at the N-terminus and achiral OAcc at the C-terminus preferentially adopted a right-handed 1.88 helical structure, but dipeptide 3 (OAcc-d-OAA) did not. Theoretical calculation results, in good agreement with experimental ones, revealed that the biased handedness of α N-O turn found in OAcc residue depends on its preceding chiral residue. It was then found that the helical conformation was destroyed in the case of oligopeptides 6 and 7 [OAA-(OAcc) n, n = 2, 3]. The crystal structure of tripeptide 8 ( iPrCO-d-OVal-OAcc-d-OVal-NHiBu) further disclosed the helical structure formed by three consecutive homochiral α N-O turns. This study has uncovered achiral aminoxy acid residues such as the OAcc unit as a useful building block to be incorporated into chiral aminoxy peptides to mimic chiral helix structure. © 2010 American Chemical Society.
Persistent Identifierhttp://hdl.handle.net/10722/168469
ISSN
2013 Impact Factor: 4.638
ISI Accession Number ID
References

 

Author Affiliations
  1. The University of Hong Kong
  2. Fudan University
DC FieldValueLanguage
dc.contributor.authorYang, Den_HK
dc.contributor.authorChang, XWen_HK
dc.contributor.authorZhang, DWen_HK
dc.contributor.authorJiang, ZFen_HK
dc.contributor.authorSong, KSen_HK
dc.contributor.authorZhang, YHen_HK
dc.contributor.authorZhu, NYen_HK
dc.contributor.authorWeng, LHen_HK
dc.contributor.authorChen, MQen_HK
dc.date.accessioned2012-10-08T03:19:21Z-
dc.date.available2012-10-08T03:19:21Z-
dc.date.issued2010en_HK
dc.identifier.citationJournal Of Organic Chemistry, 2010, v. 75 n. 14, p. 4796-4805en_HK
dc.identifier.issn0022-3263en_HK
dc.identifier.urihttp://hdl.handle.net/10722/168469-
dc.description.abstract(Figure Presented) The monomer 1 derived from achiral 1-(aminoxy) cyclopropanecarboxylic acid (OAcc) and oligopeptides 2-9 consisting of a chiral α-aminoxy acid and an achiral α-aminoxy acid such as OAcc were synthesized and their structures characterized. The eight-membered-ring intramolecular hydrogen bond, namely the α N-O turn, was formed between adjacent residues independent of their chirality. However, the helix formation was sequence-dependent. Dipeptide 2 bearing chiral α-aminoxy acid (d-OAA) at the N-terminus and achiral OAcc at the C-terminus preferentially adopted a right-handed 1.88 helical structure, but dipeptide 3 (OAcc-d-OAA) did not. Theoretical calculation results, in good agreement with experimental ones, revealed that the biased handedness of α N-O turn found in OAcc residue depends on its preceding chiral residue. It was then found that the helical conformation was destroyed in the case of oligopeptides 6 and 7 [OAA-(OAcc) n, n = 2, 3]. The crystal structure of tripeptide 8 ( iPrCO-d-OVal-OAcc-d-OVal-NHiBu) further disclosed the helical structure formed by three consecutive homochiral α N-O turns. This study has uncovered achiral aminoxy acid residues such as the OAcc unit as a useful building block to be incorporated into chiral aminoxy peptides to mimic chiral helix structure. © 2010 American Chemical Society.en_HK
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/jocen_HK
dc.relation.ispartofJournal of Organic Chemistryen_HK
dc.subject.meshAmino Acids - Chemistryen_US
dc.subject.meshCircular Dichroismen_US
dc.subject.meshCrystallography, X-Rayen_US
dc.subject.meshCyclopropanes - Chemical Synthesis - Chemistryen_US
dc.subject.meshDipeptides - Chemistryen_US
dc.subject.meshModels, Molecularen_US
dc.subject.meshMolecular Conformationen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMolecular Structureen_US
dc.subject.meshNitrogen - Chemistryen_US
dc.subject.meshNuclear Magnetic Resonance, Biomolecularen_US
dc.subject.meshOligopeptides - Chemical Synthesis - Chemistryen_US
dc.subject.meshOxygen - Chemistryen_US
dc.titleChiral α-aminoxy acid/achiral cyclopropane α-aminoxy acid unit as a building block for constructing the α N-O helixen_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/jo100810men_HK
dc.identifier.pmid20568786en_HK
dc.identifier.scopuseid_2-s2.0-77954561183en_HK
dc.identifier.hkuros181176-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77954561183&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume75en_HK
dc.identifier.issue14en_HK
dc.identifier.spage4796en_HK
dc.identifier.epage4805en_HK
dc.identifier.isiWOS:000279569500015-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridYang, D=7404800756en_HK
dc.identifier.scopusauthoridChang, XW=35319791100en_HK
dc.identifier.scopusauthoridZhang, DW=35320759400en_HK
dc.identifier.scopusauthoridJiang, ZF=36999443800en_HK
dc.identifier.scopusauthoridSong, KS=7401740599en_HK
dc.identifier.scopusauthoridZhang, YH=8379010100en_HK
dc.identifier.scopusauthoridZhu, NY=7201449530en_HK
dc.identifier.scopusauthoridWeng, LH=7102793404en_HK
dc.identifier.scopusauthoridChen, MQ=7406353075en_HK

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