Bhando, Timsy and Singh, Satish and Hade, Mangesh Dattu and Kaur, Jagdeep and `Dikshit , Kanak L (2021) Integration of VEK-30 peptide enhances fibrinolytic properties of staphylokinase. Biotechnology and applied biochemistry, 68 (2). pp. 213-220. ISSN 1470-8744
Full text not available from this repository. (Request a copy)Abstract
Staphylokinase (SAK), a 136 amino acid bacterial protein with profibrinolytic properties, has emerged as an important thrombolytic agent because of its fibrin specificity and reduced inhibition by α-2 antiplasmin. In an attempt to enhance the clot dissolution ability of SAK, a 30 amino acid peptide (VEK-30) derived from a plasminogen (Pg) binding protein (PAM), was fused at the C-terminal end of SAK with a RGD (Arg-Gly-Asp) linker. The chimeric protein, SAKVEK, was expressed in E. coli and purified as a soluble protein. Pg activation by equimolar complexes of SAKVEK and SAK with plasmin revealed that the fusion of VEK-30 peptide has significantly enhanced the catalytic activity of SAK. The kinetic constant, kcat /Km , of SAKVEK for the substrate Pg appeared 2.7 times higher than that of SAK and the time required for the fibrin and platelet rich clot lysis was shortened by 30% and 50%, respectively. The binary activator complex of SAKVEK with plasmin gets inhibited by α2- antiplasmin but remains protected in the presence of fibrin, very similar to SAK. Thus, the present study suggests that SAKVEK is more potent and effective as a thrombolytic agent due to its higher catalytic activity for Pg activation in a fibrin-specific manner and its ability to clear platelet-rich plasma clot faster than SAK.
| Item Type: | Article |
|---|---|
| Additional Information: | The copyright of this article belongs to Wiley |
| Uncontrolled Keywords: | VEK-30 peptide; clot lysis; fibrin; plasmin; plasminogen; staphylokinase |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 26 Jul 2022 04:08 |
| Last Modified: | 26 Jul 2022 04:08 |
| URI: | http://crdd.osdd.net/open/id/eprint/3007 |
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