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

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TitleChiral α-aminoxy acid/achiral cyclopropane α-aminoxy acid unit as a building block for constructing the α N-O helix
AuthorsYang, D1 2
Chang, XW2
Zhang, DW2
Jiang, ZF1
Song, KS1
Zhang, YH1
Zhu, NY1
Weng, LH2
Chen, MQ2
Issue Date2010
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/joc
CitationJournal Of Organic Chemistry, 2010, v. 75 n. 14, p. 4796-4805 [How to Cite?]
DOI: http://dx.doi.org/10.1021/jo100810m
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.
ISSN0022-3263
2011 Impact Factor: 4.45
2011 SCImago Journal Rankings: 0.351
DOIhttp://dx.doi.org/10.1021/jo100810m
ReferencesReferences in Scopus
DC Field
Value
dc.contributor.authorYang, D
dc.contributor.authorChang, XW
dc.contributor.authorZhang, DW
dc.contributor.authorJiang, ZF
dc.contributor.authorSong, KS
dc.contributor.authorZhang, YH
dc.contributor.authorZhu, NY
dc.contributor.authorWeng, LH
dc.contributor.authorChen, MQ
dc.date.accessioned2012-10-08T03:19:21Z
dc.date.available2012-10-08T03:19:21Z
dc.date.issued2010
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.
dc.description.natureLink_to_subscribed_fulltext
dc.identifier.citationJournal Of Organic Chemistry, 2010, v. 75 n. 14, p. 4796-4805 [How to Cite?]
DOI: http://dx.doi.org/10.1021/jo100810m
dc.identifier.doihttp://dx.doi.org/10.1021/jo100810m
dc.identifier.epage4805
dc.identifier.issn0022-3263
2011 Impact Factor: 4.45
2011 SCImago Journal Rankings: 0.351
dc.identifier.issue14
dc.identifier.pmid20568786
dc.identifier.scopuseid_2-s2.0-77954561183
dc.identifier.spage4796
dc.identifier.urihttp://hdl.handle.net/10722/168469
dc.identifier.volume75
dc.languageeng
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/joc
dc.publisher.placeUnited States
dc.relation.ispartofJournal of Organic Chemistry
dc.relation.referencesReferences in Scopus
dc.subject.meshAmino Acids - Chemistry
dc.subject.meshCircular Dichroism
dc.subject.meshCrystallography, X-Ray
dc.subject.meshCyclopropanes - Chemical Synthesis - Chemistry
dc.subject.meshDipeptides - Chemistry
dc.subject.meshModels, Molecular
dc.subject.meshMolecular Conformation
dc.subject.meshMolecular Sequence Data
dc.subject.meshMolecular Structure
dc.subject.meshNitrogen - Chemistry
dc.subject.meshNuclear Magnetic Resonance, Biomolecular
dc.subject.meshOligopeptides - Chemical Synthesis - Chemistry
dc.subject.meshOxygen - Chemistry
dc.titleChiral α-aminoxy acid/achiral cyclopropane α-aminoxy acid unit as a building block for constructing the α N-O helix
dc.typeArticle
Author Affiliations
  1. The University of Hong Kong
  2. Fudan University