A computational study of glutathione and its fragments: N-acetylcisteinylglycine and γ-glutamylmethylamide

Probing the coordination properties of glutathione with transition metal ions (Cr2+,Mn2+,Fe2+,Co2+, Ni2+,Cu2+,Zn2+,Cd2+,Hg2+) by density functional theory

“…The folded form in the gas phase is more stable than the extended form, while in aqueous solutions the extended form is more stable because of hydrogen bonds between the water molecules and GSH [41]. A recent B3LYP quantummechanical investigation found that hydrogen bonding interactions between the terminal ends of glutathione resulted in a "basket-like" conformation and this basket-conformation was one of the most stable structures in the gas phase [48]. The aim of our work goes beyond the conformational aspects of GSH.…”

“…The aim of our work goes beyond the conformational aspects of GSH. Thus, here, the stable structure ("basket-like" conformation) of GSH is considered [48] (shown in Fig. 1) and only the GSH: M + stoichiometric ratio of 1:1 has been taken into account.…”

Conformational Study of GSH and GSSG Using Constant-pH Molecular Dynamics Simulations

“…66,74,78 More recently, several authors have been trying to model GSH conformational space using molecular dynamics (MD) 67−70 and/or first principles methods. [63][64][65][66]71,72 One of the most extensive conformational analyses of GSH in water using MD was done by Rauk and co-workers. 67 Unfortunately, these authors were not able to explicitly introduce pH in their simulations.…”

“…The structure of GSH has been determined by both NMR spectroscopy and X-ray crystallography isolated − and bound to different proteins. − Also, there are several computational studies addressing GSH conformational preferences using molecular mechanics and quantum mechanics methodologies. − As most small peptides, GSH does not present a specific structure in solution, but rather an ensemble of conformations which vary according to different factors like protein and membrane interactions, or pH . In fact, due to its 4 titrable sites, the reduced GSH conformational space should be significantly affected by the solution pH.…”

“…In fact, due to its 4 titrable sites, the reduced GSH conformational space should be significantly affected by the solution pH. The p K a values of GSH have been determined by several authors using NMR spectroscopy − or potentiometry. , NMR data was also used to infer on the conformational preferences of the tripeptide. ,, More recently, several authors have been trying to model GSH conformational space using molecular dynamics (MD) − and/or first principles methods. − ,, One of the most extensive conformational analyses of GSH in water using MD was done by Rauk and co-workers . Unfortunately, these authors were not able to explicitly introduce pH in their simulations.…”