BDB -BiopanningDataSet Details

Biopanning Data

BiopanningDataSet ID: 1194

Peptides:

Sequences

VTWRMWYVPA(2)
VVHMRYSFRI(5)
YEIRFRYLQF(4)
TGYRLVIYRL(1)
ASTIRISFFV(3)
AIRIVIATNI(3)
SEGAVVFHAT(2)
KIQLQWIVSL(2)
YSGSLVLIVR(2)
SHSLKLTLVI(4)
MMKVVFRWSD(1)
TLGGGLLLWH(1)
VPVLHWTVMF(1)
RVVYISAMVT(1)
LVVINITYDR(1)
AWTSPVDSFQ(1)
YLHIVFQVPT(1)
PRGYWLRIEW(1)

Sequences Features:

Motif:

RMRY

Unique Sequence Number:

Experimental Method:

Phage display (common panning)

Sequencing Platform:

Sequencing Method:

Sanger sequencing

Rounds of Panning:

Reference:

PMID: 9531425

Target Name:

Cholesteryl ester transfer protein

Template Name:

Cholesteryl esters, CE

Structure of Target-Template Complex:

Not determined.

Structure of Target-Peptide Complex:

Not determined.

Library Name:

X10 phage display library

Affinity Measurement Method:

Affinity Measurement Description:

Brief Description:

BiopanningDataSet Comments:

Of the 36 randomly chosen clones, phage displaying VTWRMWYVPA, VVHMRYSFRI, YEIRFRYLQF and TGYRLVIYRL exhibited relatively high binding to CETP (OD450 0.4-0.7), whereas the remaining 24 clones displayed only moderate to low binding to CETP in the reported assay system. The synthesized VTWRMWYVPA inhibited CETP-catalyzed transfer of cholesteryl esters and triglycerides. Amino- and ciirboxy-terminal truncations 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, WRMWY bound directly to CETP and its inhibition was consistent with that of a competitive inhibitor of CETP.

Curator:

Curation Date:

0000-00-00

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