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.
