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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
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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, D2 1
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
2013 Impact Factor: 4.638
 
DOIhttp://dx.doi.org/10.1021/jo100810m
 
ReferencesReferences in Scopus
 
DC FieldValue
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.hkuros181176
 
dc.identifier.issn0022-3263
2013 Impact Factor: 4.638
 
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
 
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<item><contributor.author>Yang, D</contributor.author>
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<contributor.author>Zhang, DW</contributor.author>
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<contributor.author>Song, KS</contributor.author>
<contributor.author>Zhang, YH</contributor.author>
<contributor.author>Zhu, NY</contributor.author>
<contributor.author>Weng, LH</contributor.author>
<contributor.author>Chen, MQ</contributor.author>
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<description.abstract>(Figure Presented) The monomer 1 derived from achiral 1-(aminoxy) cyclopropanecarboxylic acid (OAcc) and oligopeptides 2-9 consisting of a chiral &#945;-aminoxy acid and an achiral &#945;-aminoxy acid such as OAcc were synthesized and their structures characterized. The eight-membered-ring intramolecular hydrogen bond, namely the &#945; N-O turn, was formed between adjacent residues independent of their chirality. However, the helix formation was sequence-dependent. Dipeptide 2 bearing chiral &#945;-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 &#945; 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 &#945; 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. &#169; 2010 American Chemical Society.</description.abstract>
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Author Affiliations
  1. The University of Hong Kong
  2. Fudan University