Bisphenol TMC disrupts the structure and esterase-like function of human serum albumin: Implications for the safety of BPA alternatives

Wei Zhang

doi:10.1016/j.ijbiomac.2026.151966

Bisphenol TMC disrupts the structure and esterase-like function of human serum albumin: Implications for the safety of BPA alternatives

2026-04-11

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PRE

AI

W

Wei Zhang

J

Jinqi Yang

D

Dongqin Wang

M

Mengqi Li

S

S. C. Wu

X

Xun Tuo *

DOI：10.1016/j.ijbiomac.2026.151966

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Abstract

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• BPTMC spontaneously bound to HSA driven primarily by hydrophobic interactions. • BPTMC could alter the conformation of HSA and reduce its stability. • BPTMC derivatives effectively inhibit HSA aggregation as evident by AFM analysis. • The esterase-like activity of HSA was activated by BPTMC. • Energy decomposition analysis highlights Lys199 as the critical residue.

Keywords:

BPTMC

HSA

hydrophobic interactions

esterase-like activity

Lys199

Bisphenol TMC disrupts the structure and esterase-like function of human serum albumin: Implications for the safety of BPA alternatives

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