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Molecular and thermodynamic basis for EGCG‐Keratin interaction‐part I: Molecular dynamics simulations
Author(s) -
Marzinek Jan K.,
Lian Guoping,
Marzinek Jan K.,
Mantalaris Athanasios,
Pistikopoulos Efstratios N.,
Zhao Yanyan,
Han Lujia,
Chen Longjian,
Bond Peter J.,
Noro Massimo G.
Publication year - 2013
Publication title -
aiche journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.958
H-Index - 167
eISSN - 1547-5905
pISSN - 0001-1541
DOI - 10.1002/aic.14220
Subject(s) - molecular dynamics , chemistry , thermodynamic integration , keratin , binding energy , molecule , umbrella sampling , hydrogen bond , computational chemistry , hydrophobic effect , chemical physics , thermodynamics , organic chemistry , physics , atomic physics , medicine , pathology
Nonspecific binding of small molecules to proteins influences transdermal permeation and intestinal absorption, yet understanding of the molecular and thermodynamic basis is still limited. In this study, we report all‐atom, fully solvated molecular dynamics simulations of the thermodynamic characteristics of epigallocatechin‐3‐gallate (EGCG) binding keratin. Experimental validation is reported in Part II. Herein, 18 µs of simulation sampling was calculated. We show that the binding process is a combination of hydrophobic interaction, hydrogen bonding and aromatic interaction. The umbrella sampling technique was used to calculate the binding free energy of EGCG with keratin segments. By extracting EGCG from the keratin‐EGCG complex using steered molecular dynamics, the rupture force was observed to be linearly related to the binding free energy. Multilayer binding of EGCG clusters to keratin has been shown. The binding free energy of −6.2 kcal mol −1 obtained from the simulations was in excellent agreement with the experimental Part II. © 2013 American Institute of Chemical Engineers AIChE J , 59: 4816–4823, 2013