Development of High Functional Collagen Peptide Materials using Skate Skins

During the past 10 years we have carried out liver biopsies on haemophiliacs with biochemical evidence of chronic liver disease (CLD). To date 44 biopsies have been obtained from 35 patients. Histological diagnoses are Chronic Persistent Hepatitis (CPH) 24, Chronic Aggressive Hepatitis (CAH) 11 and Cirrhosis 9. Serial biopsies indicate that progressive liver disease is now a serious problem in haemophilia. Liver biopsy is not without risk and therefore it is important to identify factors which may be of value in predicting the nature of the liver disease or its progression. Since intra-hepatic fibrosis is a feature of CLD we measured Type III amino terminal propeptide of pro-collagen (PC III) by radio-immunoassay on samples taken within a mean of 4.8 months of the liver biopsy. A normal range was established as 4.3 - 15.7ng/ml on healthy subjects (median 7.0). Median values and ranges for patients with CPH (N=13), CAH (N=5) and cirrhosis (N=5) were 8 (5.4 - 23.4), 14.2 (7.2 - 19.8) and 14.2 (11.2 - 23.0)ng/ml respectively. Although pro-collagen III values tended to be higher in progressive liver disease (CAH and cirrhosis) this did not reach statistical significance. It would, therefore, appear that unlike serum IgG, pro-collagen III will not be a valuable predictor of progressive liver disease in haemophilia. A larger study is necessary to clarify this.

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Peptide Materials for Smart Therapeutic Applications

Macromolecular Research ◽

10.1007/s13233-021-9011-x ◽

2021 ◽

Vol 29 (1) ◽

pp. 2-14

Author(s):

Jeonghun Lee ◽

Chulhee Kim

Keyword(s):

Therapeutic Applications ◽

Peptide Materials

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Collagen peptide-loaded W1/O single emulsions and W1/O/W2 double emulsions: influence of collagen peptide and salt concentration, dispersed phase fraction and type of hydrophilic emulsifier on droplet stability and encapsulation efficiency

Food & Function ◽

10.1039/c8fo02467g ◽

2019 ◽

Vol 10 (6) ◽

pp. 3312-3323 ◽

Cited By ~ 5

Author(s):

Yeon-Ji Jo ◽

Heike Petra Karbstein ◽

Ulrike Sabine van der Schaaf

Keyword(s):

Salt Concentration ◽

Encapsulation Efficiency ◽

Phase Fraction ◽

Dispersed Phase ◽

Functional Ingredients ◽

Food Grade ◽

Double Emulsions ◽

Collagen Peptide ◽

Droplet Stability ◽

Formulation Parameters

Collagen peptide-loaded double emulsions are developed by using various formulation parameters to utilize as food-grade functional ingredients with excellent droplet stability and encapsulation efficiency of collagen peptide.

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Monitoring urinary collagen metabolite changes following collagen peptide ingestion and physical activity using ELISA with anti active collagen oligopeptide antibody

Scientific Reports ◽

10.1038/s41598-021-92934-1 ◽

2021 ◽

Vol 11 (1) ◽

Author(s):

Yoshihiro Osawa ◽

Kaho Nomura ◽

Yoshifumi Kimira ◽

Seiji Kushibe ◽

Ken-ichi Takeyama ◽

...

Keyword(s):

Physical Activity ◽

Student Athletes ◽

Cross Reactivity ◽

University Student ◽

Collagen Metabolism ◽

The Novel ◽

Urinary Level ◽

Collagen Peptide ◽

Urinary Levels ◽

Over Time

AbstractActive collagen oligopeptides (ACOP) are bioactive collagen-derived peptides detected by a recently-established ELISA. To facilitate studies of the function and metabolism of these products, this study aims to determine which of these peptides is recognized by a novel anti-ACOP antibody used in this ELISA. We then investigate the effect of collagen peptide (CP) ingestion and exercise on urinary ACOP concentrations in a cohort of university student athletes using colorimetric, LC–MS/MS, and ELISA. We observed that the antibody showed strong cross-reactivity to Pro-Hyp and Gly-Pro-Hyp and weak cross-reactivity to commercial CP. CP ingestion increased the urinary level of ACOP over time, which correlated highly with urinary levels of peptide forms of Hyp and Pro-Hyp. Physical activity significantly decreased the urinary ACOP level. This study demonstrates changes in urinary ACOP following oral CP intake and physical activity using ELISA with the novel anti-ACOP antibody. Thus, ACOP may be useful as a new biomarker for collagen metabolism.

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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.

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Monoclonal antibodies identify residues 199–216 of the integrin α2 vWFA domain as a functionally important region within α2β1

Biochemical Journal ◽

10.1042/bj3500485 ◽

2000 ◽

Vol 350 (2) ◽

pp. 485-493 ◽

Cited By ~ 1

Author(s):

Danny S. TUCKWELL ◽

Lyndsay SMITH ◽

Michelle KORDA ◽

Janet A. ASKARI ◽

Sentot SANTOSO ◽

...

Keyword(s):

Monoclonal Antibodies ◽

Binding Site ◽

Conformational Changes ◽

Cation Binding ◽

Inhibitory Antibody ◽

Collagen Binding ◽

Collagen Peptide ◽

Binding Residue ◽

Important Region ◽

Domain Mapping

Integrin α2β1 is the major receptor for collagens in the human body, and the collagen-binding site on the α2 subunit von Willebrand factor A-type domain (vWFA domain) is now well defined. However, the biologically important conformational changes that are associated with collagen binding, and the means by which the vWFA domain is integrated into the whole integrin are not completely understood. We have raised monoclonal antibodies against recombinant α2 vWFA domain for use as probes of function. Three antibodies, JA202, JA215 and JA218, inhibited binding to collagen, collagen I C-propeptide and E-cadherin, demonstrating that their function is important for structurally diverse α2β1 ligands. Cross-blocking studies grouped the epitopes into two clusters: (I) JA202, the inhibitory antibody, Gi9, and a non-inhibitory antibody, JA208; (II) JA215 and JA218. Both clusters were sensitive to events at the collagen binding site, as binding of Gi9, JA202, JA215 and JA218 were inhibited by collagen peptide, JA208 binding was enhanced by collagen peptide, and binding of JA202 was decreased after mutagenesis of the cation-binding residue Thr221 to alanine. Binding of cluster I antibodies was inhibited by the anti-functional anti-β1 antibody Mab13, and binding of Gi9 and JA218 to α2β1 was inhibited by substituting Mn2+ for Mg2+, demonstrating that these antibodies were sensitive to changes initiated outside the vWFA domain. Mapping of epitopes showed that JA202 and Gi9 bound between residues 212–216, while JA208 bound between residues 199–216. We have therefore identified two epitope clusters with novel properties; i.e. they are intimately associated with the collagen-binding site, responsive to conformational changes at the collagen-binding site and sensitive to events initiated outside the vWFA domain.

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