Identification and Rational Redesign of Peptide Ligands to CRIP1, A Novel Biomarker for Cancers

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Identification and Rational Redesign of Peptide Ligands to CRIP1, A Novel Biomarker for Cancers

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dc.contributor.author Hao, Jihua
dc.contributor.author Serohijos, Adrian
dc.contributor.author Newton, Gail
dc.contributor.author Tassone, Gina
dc.contributor.author Wang, Zuncai
dc.contributor.author Sgroi, Dennis Charles
dc.contributor.author Dokholyan, Nikolay V.
dc.contributor.author Basilion, James P.
dc.date.accessioned 2010-12-10T15:58:38Z
dc.date.issued 2008
dc.identifier.citation Hao, Jihua, Adrian W. R. Serohijos, Gail Newton, Gina Tassone, Zuncai Wang, Dennis C. Sgroi, Nikolay V. Dokholyan, and James P. Basilion. 2008. Identification and Rational Redesign of Peptide Ligands to CRIP1, A Novel Biomarker for Cancers. PLoS Computational Biology 4(8): e1000138. en_US
dc.identifier.issn 1553-734X en_US
dc.identifier.uri http://nrs.harvard.edu/urn-3:HUL.InstRepos:4622131
dc.description.abstract Cysteine-rich intestinal protein 1 (CRIP1) has been identified as a novel marker for early detection of cancers. Here we report on the use of phage display in combination with molecular modeling to identify a high-affinity ligand for CRIP1. Panning experiments using a circularized C7C phage library yielded several consensus sequences with modest binding affinities to purified CRIP1. Two sequence motifs, A1 and B5, having the highest affinities for CRIP1, were chosen for further study. With peptide structure information and the NMR structure of CRIP1, the higher-affinity A1 peptide was computationally redesigned, yielding a novel peptide, A1M, whose affinity was predicted to be much improved. Synthesis of the peptide and saturation and competitive binding studies demonstrated approximately a 10–28-fold improvement in the affinity of A1M compared to that of either A1 or B5 peptide. These techniques have broad application to the design of novel ligand peptides. en_US
dc.language.iso en_US en_US
dc.publisher Public Library of Science en_US
dc.relation.isversionof doi:10.1371/journal.pcbi.1000138 en_US
dc.relation.hasversion http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2453235/pdf/ en_US
dash.license LAA
dc.subject biochemistry en_US
dc.subject bioinformatics en_US
dc.subject experimental biophysical methods en_US
dc.subject protein folding en_US
dc.subject biophysics en_US
dc.subject theory and simulation en_US
dc.subject bioengineering en_US
dc.subject biotechnology en_US
dc.subject macromolecular Chemistry en_US
dc.subject macromolecular chemistry en_US
dc.subject protein structure prediction en_US
dc.subject computational biology en_US
dc.subject oncology en_US
dc.subject directed molecular evolution en_US
dc.title Identification and Rational Redesign of Peptide Ligands to CRIP1, A Novel Biomarker for Cancers en_US
dc.type Journal Article en_US
dc.description.version Version of Record en_US
dc.relation.journal PLoS Computational Biology en_US
dash.depositing.author Sgroi, Dennis Charles
dc.date.available 2010-12-10T15:58:38Z
dash.affiliation.other HMS^Pathology en_US

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