Enhanced Plasma Persistence of Enzyme with Therapeutic Potential Using Polyethylene Glycol as a Coupling Agent

Rahamat Unissa*, Sai P. Neeeraj, Vamshi K. Krishna, Machkure Gnaneshwar, Md Irshad Ayyub, Sowmya Konakanchi, Preethi K. Singh, Kavya T. Arasan
Department of Pharmaceutical Biotechnology, Faculty of Pharmacy, Malla Reddy College Of Pharmacy, Maisammaguda, Dhulapally, Secunderabad, Telangana, India
Corresponding Author: [email protected]; Tel: +91-7799290715
Recieved Date: August 24, 2017; Accepted Date: September 09, 2017; Published Date: 09 September 2017
Citation: Unissa R, Neeeraj SP, Krishna VK, Gnaneshwar M, Ayyub MI, Konakanchi S, Singh PK, Arasan KT. Enhanced Plasma Persistence of Enzyme with Therapeutic Potential Using Polyethylene Glycol as a Coupling Agent. Tropical Journal of Natural Product Research 2017; 1(3):110-112. https://doi.org/10.26538/tjnpr/v1i3.5
Copyright: © 2017 Unissa et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
ABSTRACT

Therapeutic proteins of microbial origin though possess good pharmacological activities, gets quickly broken down into amino acids by the action of proteases in the body. Hence to protect its activity and integrity the enzyme L-arginine deiminase (ADI) was coupled with a compatible polymer methoxypolyethylene glycol-succinimidyl succinate (mPEG-SS) and was further evaluated for the presence of its activity. Enzyme production was carried out by culturing Vibrio alginolyticus under optimal conditions and was purified by standard chromatographic techniques. The purified enzyme obtained was coupled with mPEG-SS 20k (1:50 mM) and purified. Coupling increased the molecular weight of the enzyme to about 112 kDa. The Km and Vmax values of immobilized enzyme were found to be 2.94 ± 0.13 mM and 129.87 ± 1.24 U/mL/min, respectively. Though there was a slight change in Km and Vmax values, it still retained its activity. Further, there was two-fold increase in the plasma half-lives of the enzymes. L-Arginine deiminase of Vibrio alginolyticus remained effective even after pegylation and showed enhanced plasma persistence in normal as well as tumour bearing mice. Hence it can be a promising candidate in treatment of L-arginine auxotrophic cancers. Further studies must be carried out to develop the enzyme in the form of chemotherapeutic agent.

Keywords: Vibrio alginolyticus, L-arginine deiminase (ADI), Pegylation, Plasma half-lives
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