Linked Life Data

7690752

Source:http://linkedlifedata.com/resource/pubmed/id/7690752

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pubmed-article:7690752pubmed:abstractTextThe alpha 5 beta 1 integrin binds fibronectin through the integrin recognition sequence Arg-Gly-Asp (RGD). We have used a 6-amino acid peptide library expressed on filamentous phage to identify peptide ligands for alpha 5 beta 1. We found that this integrin selectively binds RGD-containing peptides from the library. Of the 32 different sequences obtained, 28 had the RGD motif, 3 contained sequences related to RGD, and only 1 had a clearly different sequence. One of the RGD-containing phage encoded a potentially cyclic insert CRGDCL. The cyclic peptide GAC*RGDC*LGA (where * denotes cysteines forming a disulfide bond) was 10-fold more efficient than any of the linear RGD-containing hexapeptides in inhibiting the binding of RGD-expressing phage to alpha 5 beta 1 or the attachment of alpha 5 beta 1-expressing cells to fibronectin. This peptide also inhibited cell attachment mediated by the alpha v beta 1, alpha v beta 3, and alpha v beta 5 integrins with about 10-fold higher efficiency than linear GRGDSP. One peptide containing an RGD-related sequence, NGRAHA, was also found to inhibit phage attachment and cell adhesion, especially adhesion mediated by the alpha v beta 5 integrin. These results indicate that novel and high affinity ligands for integrins can be isolated from a random peptide library.lld:pubmed
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pubmed-article:7690752pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:7690752pubmed:articleTitleSelection of peptides binding to the alpha 5 beta 1 integrin from phage display library.lld:pubmed
pubmed-article:7690752pubmed:affiliationCancer Research Center, La Jolla Cancer Research Foundation, California 92037.lld:pubmed
pubmed-article:7690752pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:7690752pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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