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Article: The effect of backbone stereochemistry on the folding of acyclic β2,3-aminoxy peptides
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TitleThe effect of backbone stereochemistry on the folding of acyclic β2,3-aminoxy peptides
 
AuthorsZhang, YH1 2
Song, K1
Zhu, NY1
Yang, D1
 
KeywordsAminoxy acids conformation analysis
Foldamers
Peptidomimetics
Stereochemistry
 
Issue Date2010
 
PublisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/chemistry
 
CitationChemistry - A European Journal, 2010, v. 16 n. 2, p. 577-587 [How to Cite?]
DOI: http://dx.doi.org/10.1002/chem.200901471
 
AbstractAs a new type of foldamer, β-aminoxy peptides have the ability to adopt novel β N-O turns or β N-O helices in solution. Herein, we describe a new subclass of β-aminoxy peptide, that is, peptides of acyclic β2,3-aminoxy acids (NH2OCHR1CHR 2COOH), in which the presence of two chiral centers provides insight into the effect of backbone stereochemistry on the folding of β-aminoxy peptides. Acyclic β2,3aminoxy peptides with syn and anti configurations have been synthesized and their conformations investigated by NMR, IR, and circular dichroism (CD) spectroscopic, and X-ray crystallographic analysis. The ß N-O turns or β N-O helices, which feature ninemembered rings with intramolecular hydrogen bonds and have been identified previously in peptides of β3- and β2,2-aminoxy acids, are also predominantly present in the acyclic β2,3- aminoxy peptides with a syn configuration and N-O bonds gauche to the C a-Cβ bonds in both solution and the solid state. In the acyclic β2,3-aminoxy peptides with an anti configuration, an extended strand (i.e., non-hydrogenbonded state) is found in the solid state, and several conformations including non-hydrogen-bonded and intramolecular hydrogen-bonded states are present simultaneously in nonpolar solvents. These results suggest that the backbone stereochemistry does affect the folding of the acyclic β2,3-aminoxy peptides. Theoretical calculations on the conformations of model acyclic β2,3-aminoxy peptides with different backbone stereochemistry were also conducted to elucidate structural characteristics. Our present work may provide useful guidelines for the design and construction of new foldamers with predicable structures. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.
 
ISSN0947-6539
2013 Impact Factor: 5.696
 
DOIhttp://dx.doi.org/10.1002/chem.200901471
 
ISI Accession Number IDWOS:000274265100025
Funding AgencyGrant Number
University of Hong Kong
Research Grants Council of Hong KongHKU 06/2C
HKU 7654/06M
Funding Information:

This study was supported by The University of Hong Kong and the Research Grants Council of Hong Kong (HKU 06/2C and HKU 7654/06M).

 
ReferencesReferences in Scopus
 
GrantsDeveloping aminoxy acids-containing peptide mimics as small moleucle inhibitors of protein-protein interactions
 
DC FieldValue
dc.contributor.authorZhang, YH
 
dc.contributor.authorSong, K
 
dc.contributor.authorZhu, NY
 
dc.contributor.authorYang, D
 
dc.date.accessioned2011-07-14T02:04:12Z
 
dc.date.available2011-07-14T02:04:12Z
 
dc.date.issued2010
 
dc.description.abstractAs a new type of foldamer, β-aminoxy peptides have the ability to adopt novel β N-O turns or β N-O helices in solution. Herein, we describe a new subclass of β-aminoxy peptide, that is, peptides of acyclic β2,3-aminoxy acids (NH2OCHR1CHR 2COOH), in which the presence of two chiral centers provides insight into the effect of backbone stereochemistry on the folding of β-aminoxy peptides. Acyclic β2,3aminoxy peptides with syn and anti configurations have been synthesized and their conformations investigated by NMR, IR, and circular dichroism (CD) spectroscopic, and X-ray crystallographic analysis. The ß N-O turns or β N-O helices, which feature ninemembered rings with intramolecular hydrogen bonds and have been identified previously in peptides of β3- and β2,2-aminoxy acids, are also predominantly present in the acyclic β2,3- aminoxy peptides with a syn configuration and N-O bonds gauche to the C a-Cβ bonds in both solution and the solid state. In the acyclic β2,3-aminoxy peptides with an anti configuration, an extended strand (i.e., non-hydrogenbonded state) is found in the solid state, and several conformations including non-hydrogen-bonded and intramolecular hydrogen-bonded states are present simultaneously in nonpolar solvents. These results suggest that the backbone stereochemistry does affect the folding of the acyclic β2,3-aminoxy peptides. Theoretical calculations on the conformations of model acyclic β2,3-aminoxy peptides with different backbone stereochemistry were also conducted to elucidate structural characteristics. Our present work may provide useful guidelines for the design and construction of new foldamers with predicable structures. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.
 
dc.description.natureLink_to_subscribed_fulltext
 
dc.identifier.citationChemistry - A European Journal, 2010, v. 16 n. 2, p. 577-587 [How to Cite?]
DOI: http://dx.doi.org/10.1002/chem.200901471
 
dc.identifier.doihttp://dx.doi.org/10.1002/chem.200901471
 
dc.identifier.epage587
 
dc.identifier.hkuros180948
 
dc.identifier.isiWOS:000274265100025
Funding AgencyGrant Number
University of Hong Kong
Research Grants Council of Hong KongHKU 06/2C
HKU 7654/06M
Funding Information:

This study was supported by The University of Hong Kong and the Research Grants Council of Hong Kong (HKU 06/2C and HKU 7654/06M).

 
dc.identifier.issn0947-6539
2013 Impact Factor: 5.696
 
dc.identifier.issue2
 
dc.identifier.openurl
 
dc.identifier.pmid19876967
 
dc.identifier.scopuseid_2-s2.0-75649122236
 
dc.identifier.spage577
 
dc.identifier.urihttp://hdl.handle.net/10722/134737
 
dc.identifier.volume16
 
dc.languageeng
 
dc.publisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/chemistry
 
dc.publisher.placeGermany
 
dc.relation.ispartofChemistry - A European Journal
 
dc.relation.projectDeveloping aminoxy acids-containing peptide mimics as small moleucle inhibitors of protein-protein interactions
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshCrystallography, X-Ray
 
dc.subject.meshModels, Theoretical
 
dc.subject.meshMolecular Conformation
 
dc.subject.meshPeptides - chemistry
 
dc.subject.meshProtein Structure, Secondary
 
dc.subjectAminoxy acids conformation analysis
 
dc.subjectFoldamers
 
dc.subjectPeptidomimetics
 
dc.subjectStereochemistry
 
dc.titleThe effect of backbone stereochemistry on the folding of acyclic β2,3-aminoxy peptides
 
dc.typeArticle
 
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Author Affiliations
  1. The University of Hong Kong
  2. Wuhan National Laboratory for Optoelectronics