Investigation on the effect of artificial chaperones on lysozyme aggregation

Abstract

Protein misfolding and aggregation is an unwanted phenomenon occurring in cells which is one of the cause of various degenerative diseases. The conformational changes occurring due to certain environmental conditions and due to the mutations in the native state causes large amount of â sheets which are stable in the body environment because of their lower energy state. Once amyloid formation takes place lysis of these molecules becomes really difficult. Hence it is very important to stop aggregation at its very early stage. In this work modification was done on existing protocols on protein aggregation and an altogether new protocol was developed .Using this protocol, which involved denaturing of lysozyme protein at high temperatures, interference of molecules like oleic acid and sucrose were observed on the aggregates formed. Thioflavin T assay and Congo red assay were performed .Observations were monitored and recorded using fluorescence spectrophotometer and UV/VIS spectrophotometer. Oleic acid was found to accelerate the aggregation mechanism whereas sucrose was found to inhibit it. This important analysis gave important information about molecules that can be administered as drugs for inhibiting protein aggregation.