Osmolyte induced stabilization of protein molecules: a brief review.

Abstract

Cells use small molecule osmolytes to protect themselves from harsh environmental conditions. These molecules protect cellular infrastructures against denaturation and aggregation. This is important because aggregation and denaturation of cellular proteins can lead to various physiological malfunctions and life threatening diseases. Osmolytes enhance folding of different proteins, increase their stability and reduce aggregation; and hence are often termed as "chemical chaperones". The present review sheds fresh insights into the properties and mechanism of action of these interesting molecules, along with the recent concept of pharmacological chaperones. The interesting mechanism of a potent protein stabilizer arginine has also been discussed. Native conformation, generally regarded as the most stable conformation at physiological conditions, is responsible for proper functioning of a protein. Misfolded proteins having non-native conformations may not function properly, re...