Identification of ADAMTS13 peptide sequences binding to von Willebrand factor

Takanori Moriki, Ichiro N. Maruyama, Atsuko Igari, Yasuo Ikeda, Mitsuru Murata

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


ADAMTS13 cleaves multimeric von Willebrand factor (VWF) to regulate VWF-mediated thrombus formation. To search ADAMTS13 peptide sequences binding to VWF, a λ-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 Arg670 to Gln684 (epitope-A) were selected. To explore additional sites, peptide sequences from the first screening were synthesized and added to the second screening. Consequently, Pro618 to Glu641 (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.

Original languageEnglish
Pages (from-to)783-788
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 2010 Jan 1


  • ADAMTS13
  • Phage display
  • TTP
  • VWF

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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