Source:http://linkedlifedata.com/resource/pubmed/id/20812686
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
38
|
pubmed:dateCreated |
2010-9-23
|
pubmed:abstractText |
In sharp contrast with helical polypeptides carrying basic side chains, Api(8), a basic oligopeptide containing the non-natural achiral amino acid 4-aminopiperidine-4-carboxylic acid (Api), adopts a helical conformation only in acidic media. Alkaline titration of a protonated Api(8) oligomer appended with a leucine derivative at its N-terminus showed that disruption of its helical conformation occurs in a pH range of 7-10. NMR studies indicated that the piperidine groups in Api(8), when nonprotonated, possibly interact with the proximal amide protons in the peptide backbone and hamper the formation of the H-bonding network responsible for the helical conformation. The helical structure is induced not only by protonation but also by acylation of the piperidine groups.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
1520-5126
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:day |
29
|
pubmed:volume |
132
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
13176-8
|
pubmed:meshHeading | |
pubmed:year |
2010
|
pubmed:articleTitle |
Oligo(4-aminopiperidine-4-carboxylic acid): an unusual basic oligopeptide with an acid-induced helical conformation.
|
pubmed:affiliation |
Department of Chemistry and Biotechnology, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8656, Japan.
|
pubmed:publicationType |
Journal Article
|