Linked Life Data

15856432

Source:http://linkedlifedata.com/resource/pubmed/id/15856432

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2005-5-3
pubmed:abstractText
Chirality plays a central role in various biological recognition processes. Here a methodology was developed to utilize chiral recognition processes for the selective biotinylation of proteins in crude cell lysates. Two pairs of diastereomeric probes containing benzophenone and biotin were prepared through solid-phase synthesis. Protein-binding selectivity of each probe was examined by photo-cross-linking of cell lysates, followed by SDS-PAGE and Western blot. The study revealed that our approach permits selective labeling of benzophenone-binding proteins in complex proteomes. In addition, it was found that the selectivity depends largely on a single chiral center and substitutions in the vicinity of benzophenone. Taken together, the current work demonstrates that chiral recognition process can be employed to selectively label proteins in complex proteomes. Thus the study opens up the possibility to expand the scope of chemical proteomics research for various applications, including biomarker discovery, drug screening and development.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0899-0042
pubmed:author
pubmed:copyrightInfo
Copyright (c) 2005 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
332-7
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Protein fishing with chiral molecular baits.
pubmed:affiliation
Department of Chemistry, CUNY-Hunter College, New York, New York 10021, USA. akawamur@hunter.cuny.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, N.I.H., Extramural