scholarly journals Synthesis and Characterization of Wound Dressing Material from Bio-Wastes Impregnated with the Spider Web and the Ethanolic Weaves Extract of Mangifera indica (L.)

2021 ◽  
Vol 12 (2) ◽  
pp. 1998-2012
Keyword(s):  
Cost Effectiveness ◽  
Wound Dressing ◽  
Type I Collagen ◽  
Mangifera Indica ◽  
Biological Evaluation ◽  
Spectroscopic Techniques ◽  
Type I ◽  
Fish Scale ◽  
Good Efficacy ◽  
Spider Web

Substantial progress in wound therapy has not snuffed out the passion in search of innovative wound dressing materials. This work is to analyze the physiochemical characterizations and biological evaluation of a wound dressing material. A wound dressing material had been synthesized from Physiologically Clotted Fibrin (PCF), Fish Scale Collagen (FSC). Also, the wound dressing material had impregnated with the folklore medicinal impact of the Spider Web (SW) and the Ethanolic Extract of Mangifera indica (L.)(EEMI). Infrared spectroscopic techniques confirmed the presence of Type I collagen. Surface morphology established the smooth, uniform, porous, biocompatible surface of the material. Water absorption studies, porosity measurements showed the required characteristics, the antibacterial activity favored the resistance, and the ash test supported the eco-friendly environment of the wound dressing material. Human erythrocytes had reviewed biocompatibility. The supernatant of the wound dressing material at different concentrations and incubation times had determined for percent hemolysis. Plots between percent hemolysis and concentration showed the non-hemolytic behavior of the wound dressing material. The synthesized biomaterial could propose as a wound dressing material with good efficacy, cost-effectiveness, and eco-friendly. The synthesized biomaterial could have been a better wound dressing material with good efficacy, cost-effectiveness, and eco-friendly.

scholarly journals Computer-aided Identification of Synergetic Wound Healing Mechanisms Exhibited by Compounds in the Bio Synthesized Wound Dressing Material

2021 ◽  
Vol 10 (4) ◽  
pp. 2831-2842
Keyword(s):  
Wound Healing ◽  
Bioactive Compounds ◽  
Wound Dressing ◽  
Biological Activities ◽  
Mangifera Indica ◽  
Beta Carotene ◽  
Fish Scale ◽  
Spider Web ◽  
Healing Wound ◽  
Pass Online

A wound dressing material synthesized from the bio-composites of chicken fibrin, fish scale collagen impregnated with the spider web, and the ethanolic leaves extract of Mangifera indica (L.). The synthesized biomaterial was analyzed by GC-MS analysis. The present study involves identifying bioactive compounds that may heal wounds from the biosynthetic wound dressing material and the biological activities determined with the help of PASS software online prediction. PASS online software is used to explore the mechanism involved in healing wound compounds. Ten bioactive compounds identified as wound healing agents 2-methyl 4-Heptanol, 3-methoxy Hexane, Stigmasterol, Z-3,17-Octadecadien-1-ol acetate, 3-Chloro-5 Cholestene, 9,12,15 Octadecatrienoic acid 2,3 –Bis(acetyloxy) propyl ester(Z, Z, Z), Trans-Z-.alpha.-bisabolene epoxide, Beta carotene, Nopyl Acetate, 9,12 Octadecadienoic acid (Z, Z)phenylmethyl ester, and their bioactivities analyzed. Analyzed bio compounds found to exhibit wound healing mechanisms.

scholarly journals Effects of chitosan-collagen dressing on wound healing in vitro and in vivo assays

2021 ◽  
Vol 19 ◽  
pp. 228080002198969
Author(s):  
Min-Xia Zhang ◽  
Wan-Yi Zhao ◽  
Qing-Qing Fang ◽  
Xiao-Feng Wang ◽  
Chun-Ye Chen ◽  
...  
Keyword(s):  
Wound Healing ◽  
Wound Dressing ◽  
Type I Collagen ◽  
Inhibition Zone ◽  
Negative Control ◽  
Type I ◽  
Nih3t3 Cells ◽  
Post Operation

The present study was designed to fabricate a new chitosan-collagen sponge (CCS) for potential wound dressing applications. CCS was fabricated by a 3.0% chitosan mixture with a 1.0% type I collagen (7:3(w/w)) through freeze-drying. Then the dressing was prepared to evaluate its properties through a series of tests. The new-made dressing demonstrated its safety toward NIH3T3 cells. Furthermore, the CCS showed the significant surround inhibition zone than empty controls inoculated by E. coli and S. aureus. Moreover, the moisture rates of CCS were increased more rapidly than the collagen and blank sponge groups. The results revealed that the CCS had the characteristics of nontoxicity, biocompatibility, good antibacterial activity, and water retention. We used a full-thickness excisional wound healing model to evaluate the in vivo efficacy of the new dressing. The results showed remarkable healing at 14th day post-operation compared with injuries treated with collagen only as a negative control in addition to chitosan only. Our results suggest that the chitosan-collagen wound dressing were identified as a new promising candidate for further wound application.

Maturation process and characterization of a novel thermostable and halotolerant subtilisin-like protease with high collagenolytic but low gelatinolytic activity

2021 ◽  
Author(s):  
Kui Zhang ◽  
Qianqian Huang ◽  
Yu Li ◽  
Lanhua Liu ◽  
Xiao-Feng Tang ◽  
...  
Keyword(s):  
High Temperatures ◽  
Type I Collagen ◽  
Elevated Temperatures ◽  
Catalytic Domain ◽  
Ion Pairs ◽  
Gelatinolytic Activity ◽  
Type I ◽  
Fish Scale ◽  
Collagenolytic Proteases ◽  
Collagenolytic Protease

Enzymatic degradation of collagen is of great industrial and environmental significance; however, little is known about thermophile-derived collagenolytic proteases. Here, we report a novel collagenolytic protease (TSS) from thermophilic Brevibacillus sp. WF146. The TSS precursor comprises a signal peptide, an N-terminal propeptide, a subtilisin-like catalytic domain, a β-jelly roll (βJR) domain, and a prepeptidase C-terminal (PPC) domain. The maturation of TSS involves a stepwise autoprocessing of the N-terminal propeptide and the PPC domain, and the βJR rather than the PPC domain is necessary for correct folding of the enzyme. Purified mature TSS displayed optimal activity at 70°C and pH 9.0, a half-life of 1.5 h at 75°C, and an increased thermostability with rising salinity up to 4 M. TSS possesses an increased number of surface acidic residues and ion pairs, as well as four Ca 2+ -binding sites, which contribute to its high thermostability and halotolerance. At high temperatures, TSS exhibited high activity toward insoluble type I collagen and azocoll, but showed a low gelatinolytic activity, with a strong preference for Arg and Gly at the P1 and P1’ positions, respectively. Both the βJR and PPC domains could bind but not swell collagen, and thus facilitate TSS-mediated collagenolysis via improving the accessibility of the enzyme to the substrate. Additionally, TSS has the ability to efficiently degrade fish scale collagen at high temperatures. IMPORTANCE Proteolytic degradation of collagen at high temperatures has the advantages of increasing degradation efficiency and minimizing the risk of microbial contamination. Reports on thermostable collagenolytic proteases are limited, and their maturation and catalytic mechanisms remain to be elucidated. Our results demonstrate that the thermophile-derived TSS matures in an autocatalytic manner, and represents one of the most thermostable collagenolytic proteases reported so far. At elevated temperatures, TSS prefers hydrolyzing insoluble heat-denatured collagen rather than gelatin, providing new insight into the mechanism of collagen degradation by thermostable collagenolytic proteases. Moreover, TSS has the potential to be used in recycling collagen-rich wastes such as fish scales.

scholarly journals Comprehensive Assessment of Nile Tilapia Skin (Oreochromis niloticus) Collagen Hydrogels for Wound Dressings

Marine Drugs ◽  
2020 ◽  
Vol 18 (4) ◽  
pp. 178 ◽  
Author(s):  
Baosheng Ge ◽  
Haonan Wang ◽  
Jie Li ◽  
Hengheng Liu ◽  
Yonghao Yin ◽  
...  
Keyword(s):  
Wound Dressing ◽  
Type I Collagen ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Wound Dressings ◽  
Type I ◽  
Rheological Characterization ◽  
Scanning Calorimetry ◽  
Soluble Collagen ◽  
Collagen Hydrogels

Collagen plays an important role in the formation of extracellular matrix (ECM) and development/migration of cells and tissues. Here we report the preparation of collagen and collagen hydrogel from the skin of tilapia and an evaluation of their potential as a wound dressing for the treatment of refractory wounds. The acid-soluble collagen (ASC) and pepsin-soluble collagen (PSC) were extracted and characterized using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), differential scanning calorimetry (DSC), circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR) analysis. Both ASC and PSC belong to type I collagen and have a complete triple helix structure, but PSC shows lower molecular weight and thermal stability, and has the inherent low antigenicity. Therefore, PSC was selected to prepare biomedical hydrogels using its self-aggregating properties. Rheological characterization showed that the mechanical strength of the hydrogels increased as the PSC content increased. Scanning electron microscope (SEM) analysis indicated that hydrogels could form a regular network structure at a suitable PSC content. Cytotoxicity experiments confirmed that hydrogels with different PSC content showed no significant toxicity to fibroblasts. Skin repair experiments and pathological analysis showed that the collagen hydrogels wound dressing could significantly accelerate the healing of deep second-degree burn wounds and the generation of new skin appendages, which can be used for treatment of various refractory wounds.

Curcumin loaded nano graphene oxide reinforced fish scale collagen – a 3D scaffold biomaterial for wound healing applications

RSC Advances ◽  
2015 ◽  
Vol 5 (119) ◽  
pp. 98653-98665 ◽  
Author(s):  
Tapas Mitra ◽  
Piyali Jana Manna ◽  
S. T. K. Raja ◽  
A. Gnanamani ◽  
P. P. Kundu
Keyword(s):  
Tissue Engineering ◽  
Wound Healing ◽  
Graphene Oxide ◽  
Type I Collagen ◽  
Type I ◽  
Fish Scale ◽  
3D Scaffold ◽  
Engineering Research ◽  
Nano Graphene ◽  
Tissue Engineering Research

We prepare a highly stabilized nano graphene oxide functionalized with type I collagen to make a 3D scaffold as a novel platform for better tissue engineering research..

scholarly journals Effect Collagen Concentration Tilapia Scales on the Quality of Burn Ointment

2021 ◽  
pp. 87-95
Author(s):  
Muhammad Firham Ramadhan ◽  
Junianto . ◽  
Rusky Intan Pratama ◽  
Iis Rostini
Keyword(s):  
Type I Collagen ◽  
Ph Value ◽  
Quality Standard ◽  
National Standard ◽  
Control Treatment ◽  
Type I ◽  
Fish Scale ◽  
Collagen Concentration ◽  
Biomedical Material ◽  
Skin Collagen

Collagen is one of the main connective tissue animal proteins and has been widely used as a biomedical material. Collagen is divided into XIX types. Type I collagen, among others, is obtained from bone, scales and skin. Collagen derived from type I can repair tissue or accelerate tissue regeneration to heal burns. The purpose of this research was to determine the addition of fish scale collagen extract to the characteristics of the burn ointment preparation in accordance with the Indonesian National Standard (SNI) and the best quality. The method used in this research is an experimental method of Completely Randomized Design (CRD) consisting of 4 collagen addition treatments: 0%, 2%, 4% and 6% repeated 5 times. Parameters in this method include physical-chemical parameters (pH, spreadability, shelf life and homogeneity) and organoleptic parameters (appearance, aroma, texture and color). Bayes test results, the concentration of the addition of tilapia scale collagen in the ointment preparation of 4% resulted in a value close to the control treatment. The addition of 4% collagen was the best treatment compared to 2% and 6% with a pH value of 6.12, dispersion of 3.22 cm, safe ointment preparation did not change at all during 28 days of storage. Based on the results of the organoleptic test parameters, the ointment at this concentration had a homogeneous appearance, slightly yellowish white color, a distinctive smell of collagen and a semi-solid texture, this was in accordance with the quality standard of the ointment and had the best quality characteristics.

scholarly journals Human Adipose-Derived Stem Cell Secreted Extracellular Matrix Incorporated into Electrospun Poly(Lactic-co-Glycolic Acid) Nanofibrous Dressing for Enhancing Wound Healing

Polymers ◽  
2019 ◽  
Vol 11 (10) ◽  
pp. 1609 ◽  
Author(s):  
Tang ◽  
Yang ◽  
Lin ◽  
Chen ◽  
Lu ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Wound Healing ◽  
Growth Factors ◽  
Wound Dressing ◽  
Type I Collagen ◽  
Healing Process ◽  
Wound Dressings ◽  
Random Structure ◽  
Type I ◽  
Enhance Wound Healing

Wound dressing, which prevents dehydration and provides a physical barrier against infection to wound beds, can improve wound healing. The interactions between extracellular matrix (ECM) and growth factors is critical to the healing process. Electrospun nanofibers are promising templates for wound dressings due to the structure similarity to ECM of skin. Otherwise, the ECM secreted by human adipose-derived stem cells (hASCs) is rich in growth factors known to enhance wound healing. Accordingly, we propose that the PLGA nanofibrous template incorporated with hASCs-secreted ECM may enhance wound healing. In this study, PLGA nanofibrous matrixes with an aligned or a random structure were prepared by electrospinning. Human ASCs cultured on the aligned matrix had a better viability and produced a larger amount of ECM relative to that of random one. After 7 days’ cultivation, the hASCs on aligned PLGA substrates underwent decellularization to fabricate cECM/PLGA dressings. By using immunohistochemical staining against F-actin and cell nucleus, the removal of cellular components was verified. However, the type I collagen and laminin were well preserved on the cECM/PLGA nanofibrous matrixes. In addition, this substrate was hydrophilic, with appropriate mechanical strength to act as a wound dressing. The L929 fibroblasts had good activity, survival and proliferation on the cECM/PLGA meshes. In addition, the cECM/PLGA nanofibrous dressings improved the wound healing of surgically created full-thickness skin excision in a mouse model. This hASCs-secreted ECM incorporated into electrospun PLGA nanofibrous could be a promising dressing for enhancing wound healing.

Fish Scale Collagen Functionalized Thermo-Responsive Nanofibres

2020 ◽  
Vol 846 ◽  
pp. 189-194
Author(s):  
Kim Yeow Tshai ◽  
Mei Hua Chin ◽  
Siew Shee Lim ◽  
Hwei San Loh ◽  
Ernest Hsin Nam Yong ◽  
...  
Keyword(s):  
Type I Collagen ◽  
Fibre Diameter ◽  
High Viscosity ◽  
Measured Quantity ◽  
Type I ◽  
Fish Scale ◽  
Electrospinning Technique ◽  
Sem Observation ◽  
Fibrous Protein ◽  
Average Fibre Diameter

Smart thermosensitive polymer such as poly (N-isopropyl acrylamide) (PNIPAM) and dominant fibrous protein of connective tissue such as collagen (CLG) possess great potential in biomedical and tissue engineering applications. The objectives of current work aim to explore potential of PNIPAM and collagen by (i) establish a stable procedure to extract collagen from fresh water Tilapia fish scale (TFS) and (ii) fabricate PNIPAM and hybrid PNIPAM-CLG nanofibrous scaffolds through electrospinning technique and investigate their material-process-structure behaviour. Type I collagen was derived through acid hydrolysis of TFS. Electrospinning of PNIPAM was carried out with 16, 18 and 20 wt% PNIPAM concentration in methanol (MeOH) while PNIPAM-CLG was prepared through blending measured quantity of PNIPAM dissolved in water with collagen dissolved in acetic acid. Material properties, viscosity, morphology and thermo-physical behaviors of the derived collagen, electrospun PNIPAM and PNIPAM-CLG scaffolds were characterized. Results from SDS-PAGE and FTIR confirmed that the isolated TFS collagen is of type I. EDX revealed that demineralization eliminated the aluminium, magnesium, silicon and phosphorus while significantly reduced the sulfur elements from raw TFS. SEM observation of the collagen morphology shown a fluffy and fibrillary lamellae structure. Electrospun scaffolds were successfully fabricated with 16 and 18 wt% PNIPAM in MeOH. Both homogeneity and average fibre diameter (Davg) were greater in the 18 wt% PNIPAM scaffold, in which the Davg for 16 and 18 wt% were ~110 and ~131.7 nm respectively. However, PNIPAM at 20 wt% failed to be electrospun owing to its excessively high viscosity. On the other hand, SEM observation revealed that the electrospun hybrid PNIPAM-CLG scaffold has Davg of ~105.5 nm amid the presence of numerous elongated beads.

Elemental distribution analysis of type I collagen fibrils in tilapia fish scale with energy-filtered transmission electron microscope

Micron ◽  
2009 ◽  
Vol 40 (5-6) ◽  
pp. 665-668 ◽  
Author(s):  
Mitsuhiro Okuda ◽  
Masaki Takeguchi ◽  
Motohiro Tagaya ◽  
Toru Tonegawa ◽  
Ayako Hashimoto ◽  
...  
Keyword(s):  
Electron Microscope ◽  
Transmission Electron Microscope ◽  
Type I Collagen ◽  
Collagen Fibrils ◽  
Elemental Distribution ◽  
Type I ◽  
Distribution Analysis ◽  
Fish Scale ◽  
Transmission Electron

scholarly journals In Situ Localization of Two Fibrillar Collagens in Two Compact Connective Tissues by Immunoelectron Microscopy After Cryotechnical Processing

1997 ◽  
Vol 45 (1) ◽  
pp. 119-128 ◽  
Author(s):  
G. Nicolas ◽  
F. Gaill ◽  
L. Zylberberg
Keyword(s):  
Osmium Tetroxide ◽  
Type I Collagen ◽  
Freeze Substitution ◽  
Immunogold Electron Microscopy ◽  
Type I ◽  
Fish Scale ◽  
Electron Microscopic ◽  
Lr White ◽  
Fibrillar Collagens ◽  
Freeze Fixation

Two fibrillar collagens, the worm cuticular collagen and the vertebrate Type I fish scale collagen, both organized in a compact tissue, were localized by immunogold electron microscopy in resin sections after freeze-fixation and freeze-substitution. Identification of these two fibrillar collagens failed with the-use of postembedding labeling after conventional electron microscopic processing. Positive labeling of the Type I collagen was observed in sections of fish scales freeze-fixed by either slam-freezing or high-pressure freezing, freeze-substituted in acetone with or without osmium tetroxide, and embedded in LR White. The worm cuticular collagen was detected in sections of cuticle that were freeze-fixed, freeze-substituted (necessarily with osmium tetroxide added to acetone), and embedded in either LR White or Epon. It was also detected in specimens pre-fixed by aldehydes before freeze-fixation. The Type I fish scale collagen appears to be more sensitive than the fibrillar cuticular collagen of worms to the procedures employed for postembedding immunoelectron microcopy. Our results have shown that freeze-fixation and freeze-substitution preserved the antigenicity of the fibrillar collagens organized in a compact three-dimensional network, whereas immunolabeling failed after conventional electron microscopic procedures. These cryostabilization techniques appear to be of value to improve the immunolocalization of collagens.

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