Ability of fibrinogen γ-derived dodecapeptides with different sequences to bind to rat platelets

Koji Tokutomi, Toshiaki Tagawa, Maki Korenaga, Masatoshi Chiba, Tomohiro Asai, Naohide Watanabe, Shinji Takeoka, Makoto Handa, Yasuo Ikeda, Naoto Oku

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


A dodecapeptide (γ400-411) derived from a fibrinogen γ-chain carboxyl-terminal sequence recognizes specifically the active form of GPIIb/IIIa on the surface of activated platelets. For the purpose of efficient hemostasis, we previously developed ADP-encapsulated liposomes modified with human-dodecapeptide (HHLGGAKQAGDV, human-H12). On the other hand, the amino-acid sequence of H12 from rats is HHMGGSKQVGDM, having only 67% homology to that from humans. Here, we investigated the ability of rat-H12 in comparison with human-H12 to bind to platelets. Firstly, rat platelets were activated with phorbol-12-myristate-13-acetate (PMA), and the activation was confirmed by flow cytometry. Next, we evaluated the dissociation constant (Kd) of human-H12 and rat-H12 for dissociation from rat platelets by using FACS. As a result, the Kd of human-H12 and rat-H12 with respect to rat platelets was 2.78 ± 0.21 and 2.91 ± 0.22 μM, respectively. Furthermore, H12 from both species inhibited quite similarly the aggregation of rat platelets in platelet-rich plasma (PRP). These results suggest that H12 from different species with different amino acid sequences interacts similarly with GPIIb/IIIa on platelets.

Original languageEnglish
Pages (from-to)296-301
Number of pages6
JournalInternational Journal of Pharmaceutics
Issue number1-2
Publication statusPublished - 2012 Nov 15


  • Dodecapeptide
  • Fibrinogen
  • GPIIb/IIIa
  • Hemostasis
  • Human
  • Rat

ASJC Scopus subject areas

  • Pharmaceutical Science


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