Suppression of protein aggregation by gold nanoparticles: a new way to store and transport proteins

Das, Anindita and Chakrabarti, Abhijit and Das, Puspendu K (2015) Suppression of protein aggregation by gold nanoparticles: a new way to store and transport proteins. In: RSC ADVANCES, 5 (48). pp. 38558-38570.

PDF Roy_Soc_of Chem_5-38558-2015.pdf - Published Version Restricted to Registered users only Download (1MB) | Request a copy

Abstract

Suppression of the aggregation of proteins has tremendous implications in biology and medicine. In the pharmaceuticals industry, aggregation of therapeutically important proteins and peptides while stored, reduces the efficacy and promptness of action leading to, in many instances, intoxication of the patient by the aggregate. Here we report the effect of gold nanoparticles (Au-NPs) in preventing the thermal and chemical aggregation of two unrelated proteins of different size, alcohol dehydrogenase (ADH, 84 kDa) and insulin (6 kDa), respectively, in physiological pH. Our principal observation is that there is a significant reduction (up to 95%) in the extent of aggregation of ADH and insulin in the presence of gold nanoparticles (Au-NPs). Aggregation of these proteins at micromolar concentration is prevented using nanomolar or less amounts of gold nanoparticles which is remarkable since chaperones which prevent such aggregation in vivo are required in micromolar quantity. The prevention of aggregation of these two different proteins under two different denaturing environments has established the role of Au-NPs as a protein aggregation prevention agent. The extent of prevention increases rapidly with the increase in the size of the gold nanoparticles. Protein molecules get physisorbed on the gold nanoparticle surface and thus become inaccessible by the denaturing agent in solution. This adsorption of proteins on AuNPs has been established by a variety of techniques and assays.

Item Type:	Journal Article
Publication:	RSC ADVANCES
Publisher:	ROYAL SOC CHEMISTRY
Additional Information:	Copy right for this article belongs to the ROYAL SOC CHEMISTRY, THOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLAND
Department/Centre:	Division of Chemical Sciences > Inorganic & Physical Chemistry
Date Deposited:	15 Jun 2015 10:09
Last Modified:	15 Jun 2015 10:09
URI:	http://eprints.iisc.ac.in/id/eprint/51676

Actions (login required)

View Item