Nanoparticles Mediated Protein Stability in Comparison with Osmolytes: in vivo Approach

Author:

Verma R.1ORCID,Singh N.2ORCID,Chaudhuri (Chattopadhyay) P.1ORCID

Affiliation:

1. Molecular Biophysics Lab, Amity Institute of Biotechnology, Amity University, Sector 125, Noida-201313, India

2. Centre for Biomedical Engineering, Indian Institute of Technology, Hauz Khas, New Delhi-110016, India

Abstract

The native three-dimensional structure of protein is quite unstable under critical destabilizing conditions. In order to enhance the stability and activity for a proper folded environment of a protein, many stabilizing materials are added such as nanoparticles and osmolytes to an unfolded state of protein. Osmolytes are the important group of molecules which are engaged by the cell as an adaption in the severe conditions. In this communication, a comparative in vivo study is reported for imparting the status of stability and folding ability of zebrafish dihydrofolate reductase (zDHFR) protein with gold nanoparticles and various osmolytes (glycerol, glucose and betain). Present observations revealed that the interaction of gold nanoparticles (AuNPs) with bacteria at the cellular level helps in maintaining the stability of protein more effectively than osmolytes which could be used for many biological and pharmacological approaches although glycerol as an osmolyte also stabilizes the protein at a significant level.

Publisher

Asian Journal of Chemistry

Subject

General Chemistry

Reference24 articles.

1. Effect of osmotic stress and heat shock in recombinant protein overexpression and crystallization

2. C. Thapliyal and P.C. Chattopadhyay, J. Protein Proteomics, 6, 211 (2015).

3. C. Osmolytes, From Chaperoning Protein Folding to Clinical Perspec-tives, Springer: Singapore, vol, 7, Chap. 1, pp 1-34 (2017).

4. Quantification of differential efficacy of chemical chaperones in ameliorating solubilization and folding of zebrafish dihydrofolate reductase

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