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Anticoagulant Activity of Low-Molecular Weight Compounds from Heterometrus laoticus Scorpion Venom

Authors :
Thien Vu Tran
Anh Ngoc Hoang
Trang Thuy Thi Nguyen
Trung Van Phung
Khoa Cuu Nguyen
Alexey V. Osipov
Igor A. Ivanov
Victor I. Tsetlin
Yuri N. Utkin
Source :
Toxins, Vol 9, Iss 11, p 343 (2017)
Publication Year :
2017
Publisher :
MDPI AG, 2017.

Abstract

Scorpion venoms are complex polypeptide mixtures, the ion channel blockers and antimicrobial peptides being the best studied components. The coagulopathic properties of scorpion venoms are poorly studied and the data about substances exhibiting these properties are very limited. During research on the Heterometrus laoticus scorpion venom, we have isolated low-molecular compounds with anticoagulant activity. Determination of their structure has shown that one of them is adenosine, and two others are dipeptides LeuTrp and IleTrp. The anticoagulant properties of adenosine, an inhibitor of platelet aggregation, are well known, but its presence in scorpion venom is shown for the first time. The dipeptides did not influence the coagulation time in standard plasma coagulation tests. However, similarly to adenosine, both peptides strongly prolonged the bleeding time from mouse tail and in vitro clot formation in whole blood. The dipeptides inhibited the secondary phase in platelet aggregation induced by ADP, and IleTrp decreased an initial rate of platelet aggregation induced by collagen. This suggests that their anticoagulant effects may be realized through the deterioration of platelet function. The ability of short peptides from venom to slow down blood coagulation and their presence in scorpion venom are established for the first time. Further studies are needed to elucidate the precise molecular mechanism of dipeptide anticoagulant activity.

Details

Language :
English
ISSN :
20726651
Volume :
9
Issue :
11
Database :
Directory of Open Access Journals
Journal :
Toxins
Publication Type :
Academic Journal
Accession number :
edsdoj.4caacc298784436dbd4564b4a67607f2
Document Type :
article
Full Text :
https://doi.org/10.3390/toxins9110343