Precision Medicine and Human Health

Resiliency of Protein Dictates Human Health

Author(s): Tajalli Ilm Chandel, Ifrah Fareed and Rizwan Hasan Khan * .

Pp: 118-152 (35)

DOI: 10.2174/9789815223583124010009

* (Excluding Mailing and Handling)

Abstract

Proteins are functional in their three-dimensional form; any type of modification in the conformation of the protein affects its functions. Thus, the role of the proteins in the body depicts the functional ability and ensures health of an organism. Besides its presence in the body, proteins are consumed by the body in the form of dietary uptake. The free amino group of the protein in the body when interacting with the carbonyl group of the reducing sugar follows the Maillard reaction to produce hazardous by-products which is an advanced glycation end products (AGEs). The process of AGEs formation routes towards the aggregation process. Different studies have shown different aggregation pathways, some restricting the partial unfolding of the protein and the other oligomerization leading to fibril formation depending upon the conditions of the study. It is noteworthy that in in-vivo cases, glycation and aggregation are the two sides of the same coin because it is obvious that we have seen the diseased condition due to AGEs formation that also shows aggregation or vice versa. Hence, the two causative agents depend upon each other.


Keywords: Advanced glycation end products (AGEs), amyloid fibrils, human diseases, oligomer, protein.

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