Tuning the self-assembly of collagen has broad applications in the biomedical field owing to their desired biological performance as collagenous materials with tunable functionalities can further determine cellular responses. In this work, an attempt has been made to tune the self-assembly of collagen using ionic liquids, viz., imidazolium chloride (IC) and choline dihydrogen phosphate (CDHP) at its physiological pH, followed by probing assembled systems using various characterization methods.
View Article and Find Full Text PDFInt J Biol Macromol
November 2019
Type I collagen is a vital structural component of the extracellular matrix providing the connective tissues with biomechanical support. One of the interesting properties of collagen is to self-associate into fibrils. The present work aims to direct the self-assembly of collagen through different molecular forces, which are tuned on the addition of thymoquinone a well-known phytochemical.
View Article and Find Full Text PDFType I collagen is a fibrous protein, which is highly biocompatible and biodegradable and exhibits low immunogenicity with its unique feature of undergoing a spontaneous self-assembly process. However, the excessive accumulation of collagen may lead to a condition known as fibrosis in vertebrates. Recently, saturated fatty acids have gained much attention as biomedical and therapeutic agents.
View Article and Find Full Text PDFColloids Surf B Biointerfaces
October 2018
Excess collagen fibril accumulation is one of the leading causes for stroke and myocardial infarction, thus inducing interest in identifying and studying the compounds, which inhibits collagen fibril formation. Herein, inhibition of self-assembly of collagen has been studied using syringic acid and vanillic acid. These plant phytochemicals are well known antioxidants and they reduce oxidative stress as well.
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