Aspartic acid functions as carbonyl trapper to inhibit the formation of advanced glycation end products by chemical chaperone activity

摘要: Advanced glycation end products (AGEs) were implicated in pathology of numerous diseases. In this study, we present the bioactivity aspartic acid (Asp) to inhibit AGEs. Hemoglobin and bovine serum albumin (BSA) glycated with glucose, fructose, ribose presence absence Asp (100-200 μM). HbA1c inhibition was investigated using human blood characterized by micro-column ion exchange chromatography. The effect methyl glyoxal (MG) on hemoglobin BSA evaluated fluorescence spectroscopy gel electrophoresis. MG red cells morphology scanning electron micrographs. Molecular docking performed Asp. is capable inhibiting formation fluorescent AGEs reacting reducing sugars. as supplement whole reduced HbA1c% from 8.8 6.1. showed an increase inhibited thereby quenched. also affected electrophoretic mobility forming high molecular weight aggregates. Normal RBCs typical biconcave shape. modified twisted elongated shape whereas ASP tends protect RBC twisting. interacted arginine residues particularly ARG 194, 198, 217 stabilized protein complex. We conclude that has dual functions a chemical chaperone stabilize dicarbonyl trapper, it can prevent complications caused glycation.