Acrylamide is formed by Maillard reaction between sugars and proteins during baking, frying or roasting. Cumulative exposure to acrylamide may result in neurotoxicity. Such toxic effects could result from covalent modification of proteins via Michael addition reaction of acrylamide with cysteine residues. The determinants of acrylamide adduct formation and its effects on protein function are not completely understood at the molecular level. As a follow-up of previous computational studies by Carloni and coworkers, here we have performed a systematic study of known acrylamide protein targets using covalent docking. Analysis of these acrylamide-protein complexes provides insights into the determinants of cysteine reactivity, as well as the residue composition of acrylamide binding sites. Moreover, it sheds light into the molecular mechanisms by which acrylamide impairs protein function. This information could potentially be used to predict additional protein targets mediating acrylamide neurotoxicity. This project was inspired by the late Dr. Ernesto Illy.

Systematic analysis of toxic acrylamide protein targets using covalent docking

ACS Spring Meeting 2021

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