Linked Life Data

21292484

Source:http://linkedlifedata.com/resource/pubmed/id/21292484

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2011-2-21
pubmed:abstractText
A new family of peptide mimics termed 'AApeptides', which are oligomers of N-acylated-N-aminoethyl amino acids, was proposed. The design and efficient synthesis of AApeptides are described. As proof-of-the-concept, we show that AApeptides can inhibit p53/MDM2 protein-protein interaction with significant activity (IC(50)=38 ?M) and specificity. Preliminary data also demonstrates that AApeptides are resistant to enzymatic hydrolysis. With the ease of synthesis and diversification, potent bioactivity, and resistance to proteolysis, the development of sequence-specific AApeptides may expand the potential biomedical applications of peptidomimetics.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1464-3405
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Elsevier Ltd. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1469-71
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Design and synthesis of AApeptides: a new class of peptide mimics.
pubmed:affiliation
Department of Chemistry, University of South Florida, Tampa, FL 33620, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't