Astaxanthin–Zn2+ complexes and glycated human serum albumin: A molecular mechanism study for protein integrity in diabetes mellitus

Glycation of Human Serum Albumin (HSA) presents a significant challenge, disrupting its structural integrity and functional capacity, and contributing to complications in chronic metabolic diseases like diabetes mellitus. The glycated form (gHSA) is particularly concerning due to its increased flexibility and reduced stability. In this study, we explore the potential of astaxanthin-Zn 2+ complexes as molecular stabilizers that can help restore the structure of gHSA. Using a comprehensive in silico approach, we applied various techniques, including molecular docking, coarse-grained molecular dynamics simulations, and analyses of energy landscapes and residue interactions. Our findings show that the astaxanthin-Zn 2+ complex at a 3:1 M ratio significantly stabilizes gHSA, leading to improved energy landscapes and more cohesive interactions. This research not only highlights the powerful synergy between astaxanthin and Zn 2+ but also opens exciting possibilities for developing new therapeutic strategies to tackle the challenges posed by glycation in diabetes.