PMID: 9531425Apr 8, 1998Paper

A peptide inhibitor of cholesteryl ester transfer protein identified by screening a bacteriophage display library

The Journal of Peptide Research : Official Journal of the American Peptide Society
P D BoninL A Erickson

Abstract

We screened a bacteriophage display library of random decapeptides to identify peptide inhibitors of cholesteryl ester transfer protein (CETP). After affinity selection against CETP, bacteriophage-infected Escherichia coli were plated at clonal density and 36 random clones were isolated. Analysis of the relevant portion of the bacteriophage DNA from a group of 12 clones that had a relatively high affinity for CETP revealed that the corresponding amino acid sequences of the displayed peptides exhibited an ... Xaa-Arg-Met-Arg-Tyr-Xaa ... composite motif. Based on those results, decapeptides from this group were synthesized and one of them, DP1 (NH2-VTWRMWYVPA-COOH), inhibited CETP-catalyzed transfer of cholesteryl esters and triglycerides. Amino- and carboxy-terminal truncations of DP1 demonstrated that the original decapeptide could be reduced to a pentapeptide without loss of either its ability to bind to CETP or its ability to inhibit CETP-mediated lipid transfer. That pentapeptide, NH2-WRMWY-COOH (WRMWY, PNU-107368E), binds directly to CETP and its inhibition is consistent with that of a competitive inhibitor of CETP with a Ki of 164 microM. WRMWY or modified versions of this peptide may be useful in studying the interactions...Continue Reading

References

Jul 27, 1990·Science·J K Scott, G P Smith
Aug 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·S E CwirlaW J Dower
Apr 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·A S JarnaginC Fielding
Dec 1, 1994·Lipids·C L BisgaierA White
May 18, 1993·Biochemistry·T Ohnishi, S Yokoyama

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