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Article: The effect of backbone stereochemistry on the folding of acyclic β2,3-aminoxy peptides

TitleThe effect of backbone stereochemistry on the folding of acyclic β2,3-aminoxy peptides
Authors
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
Citation
Chemistry - A European Journal, 2010, v. 16 n. 2, p. 577-587 How to Cite?
Abstract
As 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.
Persistent Identifierhttp://hdl.handle.net/10722/134737
ISSN
2013 Impact Factor: 5.696
ISI Accession Number ID
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).

References
Grants

 

Author Affiliations
  1. The University of Hong Kong
  2. Wuhan National Laboratory for Optoelectronics
DC FieldValueLanguage
dc.contributor.authorZhang, YHen_HK
dc.contributor.authorSong, Ken_HK
dc.contributor.authorZhu, NYen_HK
dc.contributor.authorYang, Den_HK
dc.date.accessioned2011-07-14T02:04:12Z-
dc.date.available2011-07-14T02:04:12Z-
dc.date.issued2010en_HK
dc.identifier.citationChemistry - A European Journal, 2010, v. 16 n. 2, p. 577-587en_HK
dc.identifier.issn0947-6539en_HK
dc.identifier.urihttp://hdl.handle.net/10722/134737-
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.en_HK
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/chemistryen_HK
dc.relation.ispartofChemistry - A European Journalen_HK
dc.subjectAminoxy acids conformation analysisen_HK
dc.subjectFoldamersen_HK
dc.subjectPeptidomimeticsen_HK
dc.subjectStereochemistryen_HK
dc.subject.meshCrystallography, X-Ray-
dc.subject.meshModels, Theoretical-
dc.subject.meshMolecular Conformation-
dc.subject.meshPeptides - chemistry-
dc.subject.meshProtein Structure, Secondary-
dc.titleThe effect of backbone stereochemistry on the folding of acyclic β2,3-aminoxy peptidesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0947-6539&volume=16&issue=2&spage=577&epage=587&date=2010&atitle=The+effect+of+backbone+stereochemistry+on+the+folding+of+acyclic+β2,3-aminoxy+peptides-
dc.identifier.emailZhu, NY: nzhu@hkucc.hku.hken_HK
dc.identifier.emailYang, D: yangdan@hku.hken_HK
dc.identifier.authorityZhu, NY=rp00845en_HK
dc.identifier.authorityYang, D=rp00825en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/chem.200901471en_HK
dc.identifier.pmid19876967en_HK
dc.identifier.scopuseid_2-s2.0-75649122236en_HK
dc.identifier.hkuros180948-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-75649122236&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume16en_HK
dc.identifier.issue2en_HK
dc.identifier.spage577en_HK
dc.identifier.epage587en_HK
dc.identifier.isiWOS:000274265100025-
dc.publisher.placeGermanyen_HK
dc.relation.projectDeveloping aminoxy acids-containing peptide mimics as small moleucle inhibitors of protein-protein interactions-
dc.identifier.scopusauthoridZhang, YH=8379010100en_HK
dc.identifier.scopusauthoridSong, K=7401740599en_HK
dc.identifier.scopusauthoridZhu, NY=7201449530en_HK
dc.identifier.scopusauthoridYang, D=7404800756en_HK

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