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

Authors: Tokutomi, K  Tagawa, T  Korenaga, M  Chiba, M  Asai, T  Watanabe, N  Takeoka, S  Handa, M  Ikeda, Y  Oku, N 
Citation: Tokutomi K, etal., Int J Pharm. 2012 Nov 15;438(1-2):296-301. doi: 10.1016/j.ijpharm.2012.09.016. Epub 2012 Sep 15.
Pubmed: (View Article at PubMed) PMID:22985603
DOI: Full-text: DOI:10.1016/j.ijpharm.2012.09.016

A dodecapeptide (gamma400-411) derived from a fibrinogen gamma-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 (K(d)) of human-H12 and rat-H12 for dissociation from rat platelets by using FACS. As a result, the K(d) of human-H12 and rat-H12 with respect to rat platelets was 2.78 +/- 0.21 and 2.91 +/- 0.22 muM, 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.

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CRRD Object Information
CRRD ID: 11352706
Created: 2016-07-15
Species: All species
Last Modified: 2016-07-15
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.