scholarly journals 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 ◽  
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.

Controlled Release of Bi-Layered Malvidin Tablets Using 3D Printing Techniques

2021 ◽  
pp. 70-78
Author(s):  
Tejinder Kaur ◽  
Suruchi Singh
Keyword(s):  
Controlled Release ◽  
3D Printing ◽  
Fruits And Vegetables ◽  
Physical And Mechanical Properties ◽  
3D Printer ◽  
Anti Cancer ◽  
Printing Cost ◽  
3D Printed ◽  
Cost Efficient ◽  
3D Printing Technique

Malvidin belongs to the class of anthocyanidin, a pigment compound present in fruits and vegetables like the colored berries, flowers, and vegetables which have pigments on it and it is available commercially as malvidin chloride. Malvidin is known to possess many medicinal characteristics like anti-microbial, anti-diabetic, anti-inflammatory, anti-obesity, and anti-cancer. In this research paper, a 3D printing technique is used which evolves a 3D printer based on desktop that extrudes tablets comprising the active drug which here is malvidin our main ingredient and the other excipients which are used as binders and disintegrants. Methods which are adapted here for the formulation of 3D printed tablet make the tablets appropriate for immediate and sustained release with its definite physical and mechanical properties like hardness, friability, and weight. Tablets that are extruded by the 3D printer are controlled release bi-layer tablets. Due to involvement of 3D printer, printing cost for the bi-layered tablets found very low that makes our method as cost efficient.

scholarly journals Effect of Oral Ingestion of Low-Molecular Collagen Peptides Derived from Skate (Raja Kenojei) Skin on Body Fat in Overweight Adults: A Randomized, Double-Blind, Placebo-Controlled Trial

Marine Drugs ◽  
2019 ◽  
Vol 17 (3) ◽  
pp. 157 ◽  
Author(s):  
Young Tak ◽  
Yun Kim ◽  
Jeong Lee ◽  
Yu-Hyun Yi ◽  
Young Cho ◽  
...  
Keyword(s):  
Body Fat ◽  
Animal Studies ◽  
Controlled Trial ◽  
Intervention Group ◽  
Control Group ◽  
Double Blind ◽  
Collagen Peptides ◽  
Collagen Peptide ◽  
Skin Collagen ◽  
Overweight Adults

Recent animal studies found the potential of a collagen peptide derived from skate skin to have anti-obesity effects through the suppression of fat accumulation and regulation of lipid metabolism. However, no studies have yet been performed in humans. Here, this very first human randomized, placebo-controlled, and double-blinded study was designed to investigate the efficacy and tolerability of skate skin collagen peptides (SCP) for the reduction of body fat in overweight adults. Ninety healthy volunteers (17 men) aged 41.2 ± 10.4 years with a mean body mass index of 25.6 ± 1.9 kg/m2 were assigned to the intervention group (IG), which received 2000 mg of SCP per day or to the control group (CG) given the placebo for 12 weeks and 81 (90%) participants completed the study. Changes in body fat were evaluated using dual energy X-ray absorptiometry as a primary efficacy endpoint. After 12 weeks of the trial, the percentage of body fat and body fat mass (kg) in IG were found to be significantly better than those of subjects in CG (−1.2% vs. 2.7%, p = 0.024 and −1.2 kg vs. 0.3 kg, p = 0.025). Application of SCP was well tolerated and no notable adverse effect was reported from both groups. These results suggest the beneficial potential of SCP in the reduction of body fat in overweight adults.

scholarly journals Elucidation of Antimicrobial Silver Sulfadiazine (SSD) Blend/Poly(3-Hydroxybutyrate-co-4-Hydroxybutyrate) Immobilised with Collagen Peptide as Potential Biomaterial

Polymers ◽  
2020 ◽  
Vol 12 (12) ◽  
pp. 2979
Author(s):  
Sevakumaran Vigneswari ◽  
Tana Poorani Gurusamy ◽  
H. P. S. Abdul Khalil ◽  
Seeram Ramakrishna ◽  
Al-Ashraf Abdullah Amirul
Keyword(s):  
Cell Proliferation ◽  
Tissue Regeneration ◽  
Medical Application ◽  
Silver Sulfadiazine ◽  
Tissue Response ◽  
Fibroblast Cells ◽  
Gram Positive Bacteria ◽  
Collagen Peptide ◽  
L929 Fibroblast ◽  
Antimicrobial Performance

The quest for a suitable biomaterial for medical application and tissue regeneration has resulted in the extensive research of surface functionalization of material. Poly(3-hydroxybutyrate-co-4-hydroxybutyrate) [P(3HB-co-4HB)] is a bacterial polymer well-known for its high levels of biocompatibility, non-genotoxicity, and minimal tissue response. We have designed a porous antimicrobial silver SSD blend/poly(3HB-co-4HB)-collagen peptide scaffold using a combination of simple techniques to develop a scaffold with an inter-connected microporous pore in this study. The collagen peptide was immobilised via -NH2 group via aminolysis. In order to improve the antimicrobial performance of the scaffold, silver sulfadiazine (SSD) was impregnated in the scaffolds. To confirm the immobilised collagen peptide and SSD, the scaffold was characterized using FTIR. Herein, based on the cell proliferation assay of the L929 fibroblast cells, enhanced bioactivity of the scaffold with improved wettability facilitated increased cell proliferation. The antimicrobial activity of the SSD blend/P(3HB-co-4HB)-collagen peptide in reference to the pathogenic Gram-negative, Gram-positive bacteria and yeast Candida albicans exhibited SSD blend/poly(3HB-co-4HB)-12.5 wt% collagen peptide as significant construct of biocompatible antibacterial biomaterials. Thus, SSD blend/P(3HB-co-4HB)-collagen peptide scaffold from this finding has high potential to be further developed as biomaterial.

scholarly journals Synthesis and Biomedical Application of Hydroxyapatite as Carrier for Loading and Controlled Delivery of Antibiotics

2019 ◽  
Vol 69 (12) ◽  
pp. 3400-3405
Author(s):  
Mariana Mateescu ◽  
Sanda Maria Doncea ◽  
Iuliana Raut ◽  
Cristina Lavinia Nistor ◽  
Ioneta Codrina Bujanca
Keyword(s):  
Controlled Release ◽  
Biomedical Application ◽  
Drug Loading ◽  
Antibacterial Properties ◽  
Drug Carriers ◽  
Chemical Precipitation ◽  
Controlled Delivery ◽  
Wet Chemical ◽  
Uv Visible ◽  
Wet Chemical Precipitation

The hydroxyapatite (HA) nano and microparticles were synthesized by wet-chemical precipitation in order to use them as drug carriers for biomedical applications. Scanning Electron Microscopy (SEM), Dynamic Light Scattering (DLS) and Fourier Transform Infrared Spectroscopy (FTIR) were performed to assess their size, external morphology and chemical composition. The properties of HA particles as drug carriers for antibiotics delivery were evaluated with doxycycline and chloramphenicol. The amount of drug loading and release was determined by UV-Visible spectrophotometry. The antibacterial properties of loaded HA particles were evaluated using gram-positive Bacillus subtilis bacteria and gram-negative Pseudomonas aeruginosa bacteria. The synthesized particles of HA exhibit a high adsorption capacity (around 99%) and good controlled release properties for doxycycline. The adsorption of chloramphenicol on HA was extremely low (about 2%). According to the results, the compatibility between the drug and substrate is an important factor in the absorption process, and the hydroxyapatite is a very promising carrier for controlled release of antibiotics.

scholarly journals Prolonged Collagen Peptide Supplementation and Resistance Exercise Training Affects Body Composition in Recreationally Active Men

Nutrients ◽  
2019 ◽  
Vol 11 (5) ◽  
pp. 1154 ◽  
Author(s):  
Marius Kirmse ◽  
Vanessa Oertzen-Hagemann ◽  
Markus de Marées ◽  
Wilhelm Bloch ◽  
Petra Platen
Keyword(s):  
Body Composition ◽  
Exercise Training ◽  
Resistance Exercise ◽  
Fat Free Mass ◽  
Food Record ◽  
Resistance Exercise Training ◽  
Cross Sectional ◽  
Collagen Peptides ◽  
Collagen Peptide ◽  
Double Blinded

We aimed to determine the effects of long-term collagen peptide (CP) supplementation and resistance exercise training (RET) on body composition, strength, and muscle fiber cross-sectional area (fCSA) in recreationally active men. Fifty-seven young men were randomly and double-blinded divided into a group receiving either collagen peptides (COL, 15 g/day) or a placebo (PLA). Strength testing, bioimpedance analysis, and muscle biopsies were used prior to and after an RET intervention. Food record protocols were performed during the RET intervention. The groups trained three times a week for 12 weeks. Baseline parameters showed no differences between groups, and the external training load and dietary food intake were also similar. COL showed a significant increase in fat-free mass (FFM) compared with the placebo group (p < 0.05). Body fat mass (BFM) was unchanged in COL, whereas a significant increase in BFM was observed in PLA. Both groups showed significant increases in all strength tests, with a trend for a slightly more pronounced effect in COL. The fCSA of type II muscle fibers increased significantly in both groups without differences between the two groups. We firstly demonstrated improved body composition in healthy, recreationally active men subsequent to prolonged CP supplementation in combination with RET. As the observed increase in FFM was not reflected in differences in fCSA hypertrophy between groups, we assume enhanced passive connective tissue adaptations in COL due to CP intake.

scholarly journals Adsorption and Absorption of Collagen Peptides to Polydimethlysiloxane and Its Influence on Platelet Adhesion Flow Assays

Micromachines ◽  
2020 ◽  
Vol 11 (1) ◽  
pp. 62
Author(s):  
Matthew G. Sorrells ◽  
Keith B. Neeves
Keyword(s):  
Platelet Adhesion ◽  
Amino Acid Sequences ◽  
Poloxamer 407 ◽  
Silicon Substrates ◽  
Force Microscopy ◽  
Glycoprotein Vi ◽  
Collagen Peptides ◽  
Collagen Peptide ◽  
Peptide Adsorption ◽  
Von Willebrand

Collagen peptides are an alternative to animal derived collagens for platelet function studies under flow. The purpose of this study was to examine the use of collagen peptides in polydimethylsiloxane (PDMS) devices. Three collagen peptides with amino acid sequences and structures that capture von Willebrand factor and bind it with the platelet receptors integrin α2β1 and glycoprotein VI were patterned on glass, silicon, and PDMS. Each of these surfaces was also functionalized with tridecafluoro-1,1,2,2-tetrahydrooctyltrichlorosilane (FOTS). Surfaces were characterized by their ability to support platelet adhesion, topology by atomic force microscopy, contact angle, and peptides absorption. PDMS readily absorbs collagen peptides, depleting them from solution, thus reducing their adsorption to glass and silicon substrates when used for micropatterning. Treatment of PDMS with FOTS, but not bovine serum albumin or poloxamer 407, inhibits collagen peptide absorption and supports adsorption and platelet adhesion at venous and arterial shear rates. Similarly, FOTS treatment of glass or silicon supports collagen peptide adsorption even in the presence of untreated PDMS. In conclusion, PDMS acts as an absorptive sink for collagen peptides, rendering a non-adhesive surface for platelet adhesion and competing for peptides when used for micropatterning. The absorption of collagen peptides can be overcome by functionalization of PDMS with a fluorinated alkyl silane, thus allowing its use as a material for micropatterning or as a surface for platelet adhesion flow assays.

scholarly journals Collagen survival and its use for species identification in Holocene-lower Pleistocene bone fragments from British archaeological and paleontological sites

Antiqua ◽  
2011 ◽  
Vol 1 (1) ◽  
pp. 1 ◽  
Author(s):  
Mike Buckley ◽  
Matthew James Collins
Keyword(s):  
Species Identification ◽  
Collagen Type I ◽  
Systematic Investigation ◽  
Type I ◽  
Structural Protein ◽  
Collagen Peptides ◽  
Collagen Peptide ◽  
Peptide Mass ◽  
Lower Pleistocene ◽  
Bone Fragments

Proteins have long been known to persist in Quaternary bone fossils and are often targeted as a source of carbon used in radiocarbon dating and stable isotope analyses for determining provenance and obtaining dietary information. We have previously reported a technique using the dominant structural protein collagen (type I) as a source of genetic information for species identification in modern and relatively young (Holocene) archaeological samples. We report a systematic investigation of amino acid composition and collagen peptide mass fingerprints (PMF), for a range of samples dating back approximately 1.5 million years. Extrapolation from high temperature experimental decomposition rates predict that at a constant 10°C (the approximate mean annual air temperature in Britain today) it will take between 0.2 and 0.7 Ma for levels of collagen to fall to 1% of their original concentration in an optimal burial environment. Even when the glacial intervals of the British Quaternary are factored into the temperature calculations, the more conservative of these two estimates extends the range for collagen sequencing to the Lower Pleistocene as confirmed by the presence of collagen peptides in bones from the Weybourne Crag (~1.5 Ma). Collagen fingerprinting can extend the range of identifiable taxa present at sites with large assemblages of fragmentary bone material such as that encountered at the ~900 Ka site at Happisburgh (Norfolk, UK) recently identified as showing signs of the earliest humans in Britain.

scholarly journals A fossil protein chimera; difficulties in discriminating dinosaur peptide sequences from modern cross-contamination

2017 ◽  
Vol 284 (1855) ◽  
pp. 20170544 ◽  
Author(s):  
Michael Buckley ◽  
Stacey Warwood ◽  
Bart van Dongen ◽  
Andrew C. Kitchener ◽  
Phillip L. Manning
Keyword(s):  
Peptide Sequence ◽  
Bacterial Biofilms ◽  
Sequence Information ◽  
Cross Contamination ◽  
Laboratory Practice ◽  
True Nature ◽  
Struthio Camelus ◽  
Collagen Peptides ◽  
Collagen Peptide ◽  
Single Peptide

A decade ago, reports that organic-rich soft tissue survived from dinosaur fossils were apparently supported by proteomics-derived sequence information of exceptionally well-preserved bone. This initial claim to the sequencing of endogenous collagen peptides from an approximately 68 Myr Tyrannosaurus rex fossil was highly controversial, largely on the grounds of potential contamination from either bacterial biofilms or from laboratory practice. In a subsequent study, collagen peptide sequences from an approximately 78 Myr Brachylophosaurus canadensis fossil were reported that have remained largely unchallenged. However, the endogeneity of these sequences relies heavily on a single peptide sequence, apparently unique to both dinosaurs. Given the potential for cross-contamination from modern bone analysed by the same team, here we extract collagen from bone samples of three individuals of ostrich, Struthio camelus . The resulting LC–MS/MS data were found to match all of the proposed sequences for both the original Tyrannosaurus and Brachylophosaurus studies. Regardless of the true nature of the dinosaur peptides, our finding highlights the difficulty of differentiating such sequences with confidence. Our results not only imply that cross-contamination cannot be ruled out, but that appropriate measures to test for endogeneity should be further evaluated.

Preparation and Antioxidant Capacities of Oligochitosan-Collagen Peptide Complexe

2011 ◽  
Vol 148-149 ◽  
pp. 583-586
Author(s):  
Bin Wang ◽  
Yan Wang ◽  
Zhong Rui Li ◽  
Lin Wei Huang ◽  
You Le Qu
Keyword(s):  
Hydrophobic Interactions ◽  
Radical Scavenging Activity ◽  
Intermolecular Hydrogen Bond ◽  
Radical Scavenging ◽  
Exchange Chromatography ◽  
Detection Range ◽  
Collagen Peptides ◽  
Collagen Peptide ◽  
Peptide Complexes ◽  
New Perspective

To meet the demand of food, pharmaceutical and cosmetics industry, study on the oligosaccharide- collagen peptide complexes has both scientific significance and application values. In the text, the preparation process and antioxidant capacity of oligochitosan-collagen peptides complexes were reported. The resultes indicated that the maximum DPPH radical-scavenging activity of oligochitosan-collagen peptide complexe was reached to 19.26 % when the ratio of oligochitosan to collagen peptide was 80:20, and the activity was stronger than the oligochitosan and collagen peptide at the same concentration in the detection range. In combination with the results of ion-exchange chromatography, we could concluded that the intermolecular chain associations were formed between oligochitosan chains and collagen peptide molecules driven by the electrostatic, intermolecular hydrogen bond and hydrophobic interactions. The results opened a new perspective on the utilization of oligochitosan-collagen peptide complexes as drug, food or cosmetic additives.

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