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Improving Properties of Recombinant SsoPox by Site-Specific Pegylation

[ Vol. 22 , Issue. 12 ]

Author(s):

Harsh Parikh, Priyanka Bajaj, Rajan K. Tripathy and Abhay H. Pande   Pages 1098 - 1103 ( 6 )

Abstract:


SsoPox, a ~35 kDa enzyme from Sulfolobus solfataricus, can hydrolyze and inactivate a variety of organophosphate (OP)-compounds. The enzyme is a potential candidate for the development of prophylactic and therapeutic agent against OP-poisoning in humans. However, the therapeutic use of recombinant SsoPox suffers from certain limitations associated with the use of recombinant protein pharmaceuticals. Some of these limitations could be overcome by conjugating SsoPox enzyme with polyethylene glycol (PEG). In this study, we report generation and in vitro characterization of N-terminal mono-PEGylated rSsoPox(2p) (a variant of rSsoPox(wt) having enhanced OP-hydrolyzing activity). The enzyme was PEGylated with mPEG-propionaldehyde and the PEGylated protein was isolated using ion-exchange chromatography. Compared with the unmodified enzyme, mono-PEGylation of rSsoPox results in improvement in the thermostability and protease resistance of the enzyme. PEGylated rSsoPox(2p) can be developed as a candidate for the prevention / treatment of OP-poisoning.

Keywords:

rSsoPox, mono-PEGylation, organophosphate, protease digestion, thermostability.

Affiliation:

Department of Biotechnology, National Institute of Pharmaceutical Education and Research (NIPER), Sector 67, S.A.S. Nagar, (Mohali)-160 062, Punjab, India.

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