Interaction of collagen with chlorosulphonated paraffin tanning agents: Fourier transform infrared spectroscopic analysis and molecular dynamics simulations

TitleInteraction of collagen with chlorosulphonated paraffin tanning agents: Fourier transform infrared spectroscopic analysis and molecular dynamics simulations
Publication TypeJournal Article
Year of Publication2013
AuthorsMonti, S, Bramanti, E, Porta, VD, Onor, M, D'Ulivo, A, Barone, V
JournalPhysical Chemistry Chemical Physics
Volume15
Pagination14736–14747
ISSN14639076 (ISSN)
Keywordsanimal, Animals, Article, Cattle, chemistry, Collagen, cross linking reagent, Cross-Linking Reagents, drug derivative, Fourier Transform Infrared, Halogenation, Infrared spectroscopy, leather industry, methodology, molecular dynamics, molecular dynamics simulation, Paraffin, Protein Conformation, Spectroscopy, sulfone, Sulfones, Tanning
Abstract

The binding of chlorosulphonated paraffins to collagen triple helices is studied by means of classical molecular dynamics simulations and experimental spectroscopic techniques in order to disclose the principal characteristics of their interaction during the leather fattening process. Indeed, collagen is the main target to develop new leather modifying agents with specific characteristics, and an accurate design of the collagen binders, supported by predictive computational strategies, could be a successful tool to obtain new effective eco-compatible compounds able to impart to the leather the required functionalities and distinctive mechanical properties. Possible effects caused by the tanning agents on the collagen matrix have been identified from both experimental and theoretical points of view. Computational data in agreement with experiment have revealed that chlorosulphonated paraffins can interact favorably with the collagen residues having amine groups in their side chains (Arg, Lys, Asn and Gln) and reduce the tendency of the solvated collagen matrix to swell. However, the interference of chlorosulphonated paraffins with the unfolding process, which is operated mainly by the action of water, can be due both to covalent cross-linking of the collagen chains and intermolecular hydrogen bonding interactions involving also the hydroxyl groups of Hyp, Ser and Thr residues. This journal is © the Owner Societies 2013.

URLhttp://www.scopus.com/inward/record.url?eid=2-s2.0-84882338954&partnerID=40&md5=9642f3c96b650d0615f60ca4ff6e315d
DOI10.1039/c3cp52404c