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Identification of ADAMTS13 peptide sequences binding to von Willebrand factor.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2010 Jan 01; Vol. 391 (1), pp. 783-8. Date of Electronic Publication: 2009 Nov 26. - Publication Year :
- 2010
-
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.<br /> (Copyright 2009 Elsevier Inc. All rights reserved.)
- Subjects :
- ADAM Proteins genetics
ADAMTS13 Protein
Amino Acid Sequence
Humans
Immobilized Proteins genetics
Immobilized Proteins metabolism
Molecular Sequence Data
Peptide Fragments genetics
Peptide Fragments metabolism
Peptide Library
Protein Binding
Protein Structure, Tertiary
von Willebrand Factor genetics
ADAM Proteins metabolism
von Willebrand Factor metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 391
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 19944670
- Full Text :
- https://doi.org/10.1016/j.bbrc.2009.11.138