Abstract
Collagen contains hydroxyproline (Hyp), which is a unique amino acid. Three collagen-derived small peptides (Gly-Pro-Hyp, Pro-Hyp, and Gly-Hyp) interacting across a lipid bilayer (POPC model membrane) for cellular uptakes of these collagen-derived small peptides were studied using accelerated molecular dynamics simulation. The ligands were investigated for their binding modes, hydrogen bonds in each coordinate frame, and mean square displacement (MSD) in the Z direction. The lipid bilayers were evaluated for mass and electron density profiles of the lipid molecules, surface area of the head groups, and root mean square deviation (RMSD). The simulation results show that hydrogen bonding between the small collagen peptides and plasma membrane plays a significant role in their internalization. The translocation of the small collagen peptides across the cell membranes was shown. Pro-Hyp laterally condensed the membrane, resulting in an increase in the bilayer thickness and rigidity. Perception regarding molecular behaviors of collagen-derived peptides within the cell membrane, including their interactions, provides the novel design of specific bioactive collagen peptides for their applications.
Highlights
Collagen is one of the major in vivo proteins that constitutes approximately 30% of the proteins and is found mainly in skin, cartilage, tendons, and bone, contributing their structures and functions [1,2]
Gly-Hyp andmolecule, Gly-Pro-Hyp etration ofHyp-containing a permeant in apeptides; biologicalPro-Hyp membrane well as(dipeptides) rotation of the re(tripeptide) were demonstrated to penetrate the lipid membrane model effectively after the sulted in the higher root mean square deviation (RMSD) observed
The study using the models clarified association of epigallocatechin gallate with the lipid membrane and residing at the stable location that contributed by hydrogen bonds forming with the membrane components
Summary
Collagen is one of the major in vivo proteins that constitutes approximately 30% of the proteins and is found mainly in skin, cartilage, tendons, and bone, contributing their structures and functions [1,2]. Consumption of collagen hydrolysates has helpful effects; for example, increasing the moisture content of stratum corneum and bone density, improving joint pain, decreasing blood pressure, modulating the circulatory system [3], decreasing atherosclerotic plaques, anti-pruritus, and protection against photoaging [4]. Collagen contains hydroxyproline (Hyp), which is a unique amino acid [5]. A triple-helical collagen structure composes three alpha chains that includes a frequently repeating Gly-X-Y sequence, and the X and Y amino acid residues generally become Pro and Hyp. Glycylprolylhydroxyproline (Gly-Pro-Hyp), the tripeptide, whose sequence is specific for collagen [6].
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
