Disquisition of interaction between anti-alzheimer drugs and bovin serum albumin; a computational study

Serum albumin is the most abundant protein in the body. It is the main macromolecule contributing to the osmotic blood pressure [1] and can play a superior role in drug behavior and efficacy [2]. Many drugs and other bioactive small compounds bind reversibly to albumin [3–5], which signify Serum albumin role as carriers. In this study, the interaction of two anti-alzheimer drugs (donepezil and tacrine) with bovin serum albumin (BSA) is discussed. Utilizing molecular docking simulation helps to define the mechanism of these interactions. Docking results show that the interactions of donepezil and tacrine with BSA are mainly located in domain IIA. Moreover, the interaction energy of donepezil and tacrine with BSA is equal to -149.95 kcal/mol and -102.626 kcal/mol, respectively. The interaction of these two drugs to BSA is chiefly assign to the steric interaction and hydrogen bonds. On the other hand, alanine 290 and histidine 145, compared to the other amino acids, highly increase the stability of donepezil and tacrine when interact with BSA, respectively. The geometrical structure of tacrine is responsible for the weak binding of this drug to BSA.

کلیدواژه ها:

Bovin serum albumin (BSA) ، alzheimer disease ، Molecular docking simulation ، donepezil ، tacrine