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Identification of ADAMTS13 peptide sequences binding to von Willebrand factor.

Abstract：

:ADAMTS13 cleaves multimeric von Willebrand factor (VWF) to regulate VWF-mediated thrombus formation. To search ADAMTS13 peptide sequences binding to VWF, a lambda-phage library expressing various peptides of ADAMTS13 on the surface was screened using VWF either immobilized or in solution under static condition. By the first screening, peptides sharing the C-terminus of spacer domain from Arg(670) to Gln(684) (epitope-A) were selected. To explore additional sites, peptide sequences from the first screening were synthesized and added to the second screening. Consequently, Pro(618) to Glu(641) (epitope-B) in the middle of spacer domain was obtained from immobilized VWF condition. Synthetic epitope-B peptide inhibited the cleavage of VWF by ADAMTS13, while the synthetic epitope-A peptide did not as efficiently as epitope-B. Elimination of four amino acids from either sides of epitope-B terminus markedly reduced the inhibitory effect. These two sites in the spacer domain may play significant roles in binding to VWF.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Moriki T,Maruyama IN,Igari A,Ikeda Y,Murata M

doi

10.1016/j.bbrc.2009.11.138

subject

Has Abstract

pub_date

2010-01-01 00:00:00

pages

783-8

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(09)02334-1

journal_volume

391

pub_type

杂志文章

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