DC Field | Value | Language |
---|---|---|
dc.contributor.author | Park, JS | ko |
dc.contributor.author | Lee, Hee-Seung | ko |
dc.contributor.author | Lai, JR | ko |
dc.contributor.author | Kim, BM | ko |
dc.contributor.author | Gellman, SH | ko |
dc.date.accessioned | 2013-03-04T16:36:43Z | - |
dc.date.available | 2013-03-04T16:36:43Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2003-07 | - |
dc.identifier.citation | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, v.125, no.28, pp.8539 - 8545 | - |
dc.identifier.issn | 0002-7863 | - |
dc.identifier.uri | http://hdl.handle.net/10203/83290 | - |
dc.description.abstract | beta-Amino acid oligomers composed exclusively of homochiral trans-2-aminocyclopentanecarboxylic acid (ACPC) residues and/or related pyrrolidine-based residues are known to favor a specific helical secondary structure that is defined by 12-membered ring C=O(i)- -H-N(i+3) hydrogen bonds ("12-helix"). The 12-helix is structurally similar to the familiar alpha-helix and therefore represents a source of potential a-helix-mimics. The 12-helix will be most useful in this regard if this conformational scaffold can be employed to arrange specific sets of protein-like side chains in space. Here we examine whether the 12-helix tolerates insertion of acyclic beta-amino acid residues bearing a substituent in the alpha-position (''beta(2)-residues"). Seventeen homologous beta-peptide heptamers have been prepared in which one to four beta(2)-residues reside among ACPC and/or pyrrolidine residues. Circular dichroism comparisons suggest that beta(2)-residues have a lower 12-helical propensity than do residues preorganized by a five-membered ring, as expected, but that beta-peptides containing beta(2)-residues at one or two of the seven positions retain a significant preference for 12-helix formation. These results indicate that a limited number of beta(2)-residues can be used to introduce side chains at specific positions along the surface of a 12-helix. | - |
dc.language | English | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.subject | HELICAL SECONDARY STRUCTURE | - |
dc.subject | DE-NOVO DESIGN | - |
dc.subject | VARYING CHAIN LENGTHS | - |
dc.subject | AMINO-ACID OLIGOMERS | - |
dc.subject | AQUEOUS-SOLUTION | - |
dc.subject | TRANS-2-AMINOCYCLOPENTANECARBOXYLIC ACID | - |
dc.subject | ENANTIOSELECTIVE SYNTHESIS | - |
dc.subject | BETA(2)-AMINO ACIDS | - |
dc.subject | EFFICIENT ROUTE | - |
dc.subject | WATER | - |
dc.title | Accommodation of alpha-substituted residues in the beta-peptide 12-helix: Expanding the range of substitution patterns available to a foldamer scaffold | - |
dc.type | Article | - |
dc.identifier.wosid | 000184137900030 | - |
dc.identifier.scopusid | 2-s2.0-0038713800 | - |
dc.type.rims | ART | - |
dc.citation.volume | 125 | - |
dc.citation.issue | 28 | - |
dc.citation.beginningpage | 8539 | - |
dc.citation.endingpage | 8545 | - |
dc.citation.publicationname | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | - |
dc.identifier.doi | 10.1021/ja034180z | - |
dc.contributor.localauthor | Lee, Hee-Seung | - |
dc.contributor.nonIdAuthor | Park, JS | - |
dc.contributor.nonIdAuthor | Lai, JR | - |
dc.contributor.nonIdAuthor | Kim, BM | - |
dc.contributor.nonIdAuthor | Gellman, SH | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | HELICAL SECONDARY STRUCTURE | - |
dc.subject.keywordPlus | DE-NOVO DESIGN | - |
dc.subject.keywordPlus | VARYING CHAIN LENGTHS | - |
dc.subject.keywordPlus | AMINO-ACID OLIGOMERS | - |
dc.subject.keywordPlus | AQUEOUS-SOLUTION | - |
dc.subject.keywordPlus | TRANS-2-AMINOCYCLOPENTANECARBOXYLIC ACID | - |
dc.subject.keywordPlus | ENANTIOSELECTIVE SYNTHESIS | - |
dc.subject.keywordPlus | BETA(2)-AMINO ACIDS | - |
dc.subject.keywordPlus | EFFICIENT ROUTE | - |
dc.subject.keywordPlus | WATER | - |
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