Inhibition of platelet adhesion, thrombus formation, and fibrin formation by a potent αIIbβ3 integrin inhibitor from ticks.

ABSTRACT:

Background

Ticks puncture the skin of their hosts and secrete saliva, containing antiplatelet proteins, into the blood. Here, we studied disagregin, a potent platelet-inhibiting protein derived from the salivary glands of Ornithodoros moubata, an African soft tick. Whereas conventional αIIbβ3 antagonists contain an Arg-Gly-Asp (RGD) sequence for platelet integrin binding, disagregin contains an Arg-Glu-Asp (RED) sequence, hypothesizing a different mode of inhibitory action.

Objectives

We aimed to compare the inhibitory effects of disagregin and its RGD variant (RGD-disagregin) on platelet activation and to unravel the molecular basis of disagregin-αIIbβ3 integrin interactions.

Methods

Disagregin and RGD-disagregin were synthesized by tert-butyloxycarbonyl -base

SUBMITTER: van den Kerkhof DL 

PROVIDER: S-EPMC7845065 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature