Probing the anticancer-drug-binding-induced microenvironment alterations in subdomain IIA of human serum albumin

摘要: The binding interaction of anticancer drug (using 5-fluorouracil (FU) as an example) with the model protein human serum albumin (HSA), and FU-binding-induced microenvironment alterations in subdomain IIA HSA molecule were studied by a combination spectroscopic techniques molecular docking method. results indicated that nature forces involved between FU mainly van der Waal's hydrogen bonding interactions. These interactions resulted formation FU-HSA complex, making local more hydrophobic than its native state. Moreover, caused large conformation changes HSA, leading to increase compact α-helix structures at low concentration (less 150 μM). However, high (higher μM) made structure decreasing, probably due undergoing some sort distortion. Molecular study revealed could enter inside cavity (Sudlow's site I) proximity Trp214 residue specific Lys199 residues, causing fluorescence quenching through static mechanism. essentially provides effective way for investigating induced molecules, this approach can further be used development biomedicines assessment safety-engineered delivery.