Temperature and pH Effects on Insulin Structure: A Molecular Dynamic Approach

Background: protein misfolding and aggregation are the main causes of serious diseases; thus the study of mechanism and effective factors is necessary to find the cure. since most of the proteins have the ability to produce aggregations, available and noninfectious proteins can be studied as models. insulin is one of the best models in this field. methods: the current study evaluated the effect of three temperatures of 0°c, 37°c and 47°c and neutral and acidic ph on insulin structure and misfolding by silico simulation. an insulin structure obtained by nuclear magnetic resonance (nmr) spectroscopy is simulated by gromacs package under different conditions. the secondary structure of insulin amino acids was studied in acidic and neutral conditions. results: based on the study findings the low temperature, 0°c, and acidic condition change the structure more strongly than other mentioned conditions. the low temperature and acidic conditions seem to have the most misfolding effect on insulin structure. it is hoped to find more details about the misfolding mechanism and the inducing agents. conclusions: accordingly, it can be concluded that locally low temperatures and acidic conditions are the main suspected reasons for protein misfolding.