Bioactive Collagen Peptides Ameliorate Monoiodoacetic acid Induced Osteoarthritis in Rats

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.

Download Full-text

Surface Characterization and Physiochemical Evaluation of P(3HB-co-4HB)-Collagen Peptide Scaffolds with Silver Sulfadiazine as Antimicrobial Agent for Potential Infection-Resistance Biomaterial

Polymers ◽

10.3390/polym13152454 ◽

2021 ◽

Vol 13 (15) ◽

pp. 2454

Author(s):

Sevakumaran Vigneswari ◽

Tana Poorani Gurusamy ◽

Wan M. Khairul ◽

Abdul Khalil H.P.S. ◽

Seeram Ramakrishna ◽

...

Keyword(s):

Controlled Release ◽

Antimicrobial Agent ◽

Surface Characterization ◽

Biomedical Application ◽

Physical And Mechanical Properties ◽

Silver Sulfadiazine ◽

Salt Leaching ◽

Collagen Peptides ◽

Collagen Peptide ◽

Peptide Scaffolds

Poly(3-hydroxybutyrate-co-4-hydroxybutyrate) [P(3HB-co-4HB)] is a bacterial derived biopolymer widely known for its unique physical and mechanical properties to be used in biomedical application. In this study, antimicrobial agent silver sulfadiazine (SSD) coat/collagen peptide coat-P(3HB-co-4HB) (SCCC) and SSD blend/collagen peptide coat-P(3HB-co-4HB) scaffolds (SBCC) were fabricated using a green salt leaching technique combined with freeze-drying. This was then followed by the incorporation of collagen peptides at various concentrations (2.5–12.5 wt.%) to P(3HB-co-4HB) using collagen-coating. As a result, two types of P(3HB-co-4HB) scaffolds were fabricated, including SCCC and SBCC scaffolds. The increasing concentrations of collagen peptides from 2.5 wt.% to 12.5 wt.% exhibited a decline in their porosity. The wettability and hydrophilicity increased as the concentration of collagen peptides in the scaffolds increased. In terms of the cytotoxic results, MTS assay demonstrated the L929 fibroblast scaffolds adhered well to the fabricated scaffolds. The 10 wt.% collagen peptides coated SCCC and SBCC scaffolds displayed highest cell proliferation rate. The antimicrobial analysis of the fabricated scaffolds exhibited 100% inhibition towards various pathogenic microorganisms. However, the SCCC scaffold exhibited 100% inhibition between 12 and 24 h, but the SBCC scaffolds with SSD impregnated in the scaffold had controlled release of the antimicrobial agent. Thus, this study will elucidate the surface interface-cell interactions of the SSD-P(3HB-co-4HB)-collagen peptide scaffolds and controlled release of SSD, antimicrobial agent.

Download Full-text

Metabolomics strategy reveals the osteogenic mechanism of yak (Bos grunniens) bone collagen peptides on ovariectomy-induced osteoporosis in rats

Food & Function ◽

10.1039/c9fo01944h ◽

2020 ◽

Vol 11 (2) ◽

pp. 1498-1512 ◽

Cited By ~ 1

Author(s):

Mengliang Ye ◽

Chunhui Zhang ◽

Wei Jia ◽

Qingshan Shen ◽

Xiaojie Qin ◽

...

Keyword(s):

Underlying Mechanism ◽

Bone Collagen ◽

Targeted Metabolomics ◽

First Report ◽

Bos Grunniens ◽

Collagen Peptides ◽

Positive Effect

This is the first report on the positive effect and underlying mechanism of yak bone collagen peptides in the treatment of osteoporotic rats based on non-targeted metabolomics.

Download Full-text

Isolation and characterization of pepsin-solubilized human basement membrane (type IV) collagen peptides

Biochemistry ◽

10.1021/bi00290a010 ◽

1983 ◽

Vol 22 (21) ◽

pp. 4940-4948 ◽

Cited By ~ 11

Author(s):

Robert S. MacWright ◽

Virginia A. Benson ◽

Katherine T. Lovello ◽

Michel Van der Rest ◽

Peter P. Fietzek

Keyword(s):

Basement Membrane ◽

Type Iv Collagen ◽

Collagen Peptides ◽

Type Iv ◽

Isolation And Characterization ◽

Membrane Type

Download Full-text

Screening for novel cell adhesive regions in bovine Achilles tendon collagen peptides

Biochemistry and Cell Biology ◽

10.1139/bcb-2013-0026 ◽

2014 ◽

Vol 92 (1) ◽

pp. 9-22 ◽

Cited By ~ 6

Author(s):

Pradipta Banerjee ◽

Alka Mehta ◽

C. Shanthi

Keyword(s):

Cell Adhesion ◽

Docking Studies ◽

Exchange Chromatography ◽

Adhesion Assay ◽

Structural Protein ◽

Cell Adherence ◽

Collagen Peptides ◽

Adhesion Ability ◽

A Cell ◽

Hydrophilic Residues

Collagen, a major structural protein of the ECM, is known for its high cell adherence capacity. This study was conducted to identify regions in collagen that harbour such bioactivity. Collagen from tendon was hydrolysed and the peptides fractionated using ion-exchange chromatography (IEC). Isolated peptide fractions were coated onto disposable dishes and screened for cell adherence and proliferative abilities. Active IEC fractions were further purified by chromatography, and two peptides, C2 and E1 with cell adhesion ability, were isolated. A cell adhesion assay done with different amounts of C2 coated onto disposable dishes revealed the maximum adhesion to be 94.6%, compared with 80% for collagen coated dishes and an optimum peptide coating density of 0.507 nmoles per cm2 area of the dish. Growth of cells on C2, collagen, and E1 revealed a similar pattern and a reduction in the doubling time compared with cells grown on uncoated dishes. C2 had a mass of 2.046 kDa with 22 residues, and sequence analysis revealed a higher percentage occurrence of hydrophilic residues compared with other regions in collagen. Docking studies revealed GDDGEA in C2 as the probable site of interaction with integrins α2β1 and α1β1, and stability studies proved C2 to be mostly protease-resistant.

Download Full-text