An Overview of the Use of Equine Collagen as Emerging Material for Biomedical Applications (original) (raw)
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An insight on type I collagen from horse tendon for the manufacture of implantable devices
International Journal of Biological Macromolecules, 2020
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Biomaterials, 2004
Collagen-based scaffolds are appealing products for the repair of cartilage defects using tissue engineering strategies. The present study investigated the species-related differences of collagen scaffolds with and without 1-ethyl-3-(3-dimethyl aminopropyl) carbodiimide (EDC)/N-hydroxysuccinimide (NHS)-crosslinking. Resistance against collagenase digestion, swelling ratio, amino acid sequence, shrinkage temperature, ultrastructural matrix morphology, crosslinking density and stress-strain characteristics were determined to evaluate the physico-chemical properties of equine-and bovine-collagen-based scaffolds. Three-factor ANOVA analysis revealed a highly significant effect of collagen type (p ¼ 0:0001), crosslinking (p ¼ 0:0001) and time (p ¼ 0:0001) on degradation of the collagen samples by collagenase treatment. Crosslinked equine collagen samples showed a significantly reduced swelling ratio compared to bovine collagen samples (po0:0001). The amino acid composition of equine collagen revealed a higher amount of hydroxylysine and lysine. Shrinkage temperatures of non-crosslinked samples showed a significant difference between equine (60 C) and bovine collagen (57 C). Three-factor ANOVA analysis revealed a highly significant effect of collagen type (p ¼ 0:0001), crosslinking (p ¼ 0:0001) and matrix condition (p ¼ 0:0001) on rupture strength measured by stress-strain analysis. The ultrastructure, the crosslinking density and the strain at rupture between collagen matrices of both species showed no significant differences. For tissue engineering purposes, the higher enzymatic stability, the higher form stability, as well as the lower risk of transmissible disease make the case for considering equine-based collagen. This study also indicates that results obtained for scaffolds based on a certain collagen species may not be transferable to scaffolds based on another, because of the differing physicochemical properties. r
Equine Collagen | Encyclopedia
2020
Collagen is the body’s cement that keeps everything in place . With its 28-members family it is the most important protein of vertebrates’ connective tissues that accounts for the 30% of the total body protein content . Among collagens, fibril-forming type I subspecies is the most abundant since it accounts for the 70% of the whole family . The structure of type I collagen, distributed at the level of all tissues in the organism, is known from 1938 . It consists in three right-handed polyproline-II helices of about 1000 amino acids (called α strand) that by mean of interchain hydrogen bonds are held together in a left-handed triple helix . As it is already known, each α strand is characterized by the repetition of the Gly-X-Y triplet, where the “X” and “Y” positions are usually occupied by proline and hydroxyproline . In this neat sequence, glycine plays a key role in the three α strand packing , while proline and hydroxyproline cover a fundamental role in stabilizing the triple hel...
Frontiers in Bioengineering and Biotechnology, 2019
The aim of this work is to evaluate the effects of different extraction and material processing protocols on the collagen structure and hierarchical organization of equine tendons. Wide and Small Angle X-ray Scattering investigations on raw powders and thin films revealed that not only the extraction and purification treatments, but also the processing conditions may affect the extent of the protein crystalline domain and induce a nanoscale "shield effect." This is due to the supramolecular fiber organization, which protects the atomic scale structure from the modifications that occur during fabrication protocols. Moreover, X-ray analyses and Fourier Transform Infrared spectroscopy performed on the biomaterial sheds light on the relationship between processing conditions, triple helical content and the organization in atomic and nanoscale domains. It was found that the mechanical homogenization of the slurry in acidic solution is a treatment that ensures a high content of super-organization of collagen into triple helices and a lower crystalline domain in the material. Finally, mechanical tensile tests were carried out, proving that the acidic solution is the condition which most enhances both mechanical stiffness and supramolecular fiber organization of the films.
Extraction and characterization of collagen from rabbit skin: partial characterization
CyTA - Journal of Food, 2014
Extraction and characterization of collagen were carried out in rabbit skins as a new alternative for collagen type I. Acetic acid and pepsin were for the extraction of soluble and insoluble collagen, respectively. The enzymatic treatment yielded higher amount of collagen (71%). The average pH value was 6.3, no matter what the method of extraction was. Denaturation temperature of collagen was found at 36°C approximately in two different techniques: Rheometer and Differential Scanning Calorimetry (DSC). Despite the amount of collagen in solution was low, its viscosity was high because of the hydrodynamic behaviour of collagen molecules. Sodium dodecyl sulphate polyacrylamide gel electrophoresis results showed three different bands that reflected two alpha-chains and one beta-chain with molecular weights of 102, 118 and 220 kDa, respectively. Determination of hydroxyproline gave evidence that the extracted material was collagen. It was concluded that rabbit skin could be an alternative source for the extraction of collagen.
Extraction and Characterization of Collagen from Buffalo Skin for Biomedical Applications
Oriental journal of chemistry, 2016
Collagen is widely used for biomedical and pharmaceutical applications due to its excellent biocompatibility, biodegradability and weak antigenicity. However, applicability is limited due to its high cost and probability of disease transmission from the current sources, which are bovine and porcine. In the present study, collagen was extracted from 6 months buffalo skins as alternative save sources. Collagen was characterized by different physico-chemical techniques like ATR-FTIR, Raman, SEM, DSC and amino acids analysis. Proline and hydroxyproline contents of buffalo skin collagen were higher than those of calf skin collagen. Thermal stability of buffalo skin collagen is high with respect to that of calf skin collagen. The obtained buffalo skin collagen shows higher stiffness upon cross-linking with glutaraldehyde. Thus buffalo skin collagen can be used for fabrication of high strength bioactive sponge and sheets for medical applications, like scaffold for tissue engineering, drug delivery and wound dressing system.
Collagen and Its Modifications-Crucial Aspects with Concern to Its Processing and Analysis
Macromolecular Materials and Engineering, 2017
scaffolds; however, they also make up the key proteins for a range of vital processes at work within the organism. [1] To date, some 30 various types of collagen have been identified. [2] The most abundant collagens consist of so-called fibrilforming collagens (up to 90% of all human collagens) with their characteristic quarter-staggered fibril-array. [3] The most abundant collagens are type I which is present mainly in bone, tendons, skin, dentin, etc., type II mostly in cartilage and type III like in skin. [2] The other minor collagen types are rather organ-specific. Water performs an elemental function in terms of the conservation of the physical properties of collagen. An amount of water at a level of around 20% of the total weight of collagen is necessary for the maintaining of its physical properties. In low hydrated or dehydrated collagen, the polypeptide chains are restricted in their motion; however, with increasing hydration these chains are gradually released. [1] Many connective tissue diseases and defects are associated with poor synthesis or excessive degradation of collagen. The modern tissue engineering approach is to replace the defective site via the implantation of a biocompatible scaffold which serves as a carrier for cell incorporation, proliferation, and growth. Collagen is widely used in the field of clinical medicine in connection with both hard and soft tissue applications. However, certain collagen properties such as poor dimensional stability, poor in vivo mechanical strength, low degree of elasticity, variable nature in terms of enzymatic degradation, crosslinking density, fiber size, trace impurities, and side effects frequently limit both its analysis and application. This review focuses particularly on the processing and modification of collagen type I with respect to its biological and mechanical properties. The processing of collagen into scaffolds is crucial to mimic successfully the extracellular matrices. Moreover, the review suggests several ways in which the most common problems related to the isolation, handling, electrospinning, and crosslinking of collagen can be overcome while maintaining its native character as much as possible. Further, the review provides a summary of the analytical methods available for the physicochemical characterization of collagen with respect to both its molecular and submolecular structure.
Pharmaceutics
Herein, the synthesis and characterization of a novel composite biopolymer scaffold—based on equine type I collagen and hyaluronic acid—were described by using a reaction in heterogeneous phase. The resulting biomimetic structure was characterized in terms of chemical, physical, and cytotoxicity properties using human-derived lymphocytes and chondrocytes. Firstly, FT-IR data proved a successful reticulation of hyaluronic acid within collagen structure with the appearance of a new peak at a wavenumber of 1735 cm−1 associated with ester carbonyl stretch. TGA and DSC characterizations confirmed different thermal stability of cross-linked scaffolds while morphological analysis by scanning electron microscopy (SEM) suggested the presence of a highly porous structure with open and interconnected void areas suitable for hosting cells. The enzymatic degradation profile confirmed scaffold higher endurance with collagenase as compared with collagen alone. However, it was particularly interest...
Polymers
Wound care management is incredibly challenging for chronic injuries, despite the availability of various types of wound care products in the market. However, most current wound-healing products do not attempt to mimic the extracellular matrix (ECM) and simply provide a barrier function or wound covering. Collagen is a natural polymer that involves a major constituent of the ECM protein, thus making it attractive to be used in skin tissue regeneration during wound healing. This study aimed to validate the biological safety assessments of ovine tendon collagen type-I (OTC-I) in the accredited laboratory under ISO and GLP settings. It is important to ensure that the biomatrix will not stimulate the immune system to produce any adverse reaction. Therefore, we successfully extracted collagen type-I from the ovine tendon (OTC- I) using a method of low-concentration acetic acid. The three-dimensional (3D) skin patch of spongy OTC-I was a soft and white colour, being tested for safety and ...
Biomaterials, 1991
The in viva degradation of hexamethylenediisocyanate-tanned dermal sheep collagen was studied with transmission electron microscopy. Discs of hexamethylenediisocyanate-tanned dermal sheep collagen were subcutaneously implanted in rats. Both an intra-and an extracellular route of degradation could be distinguished. In addition to normal components of a typical foreign body reaction, remarkable phenomena, such as locally deviant neutrophil morphology, infiltration of basophil-like cells, indications of foreign body multinucleate giant cells formed from different cell types, aluminium silicate accumulations and calcium phosphate depositions, were observed. Foreign body multinucleate giant cells intracellularly degraded hexamethylenediisocyanate-tanned dermal sheep collagen after internalization. Both internalized and cellularly enveloped hexamethylenediisocyanate-tanned dermal sheep collagen degraded by the detachment of fibrils. Another extracellular route of degradation was characterized by calcium phosphate depositions in large bundles of hexamethylenediisocyanate-tanned dermal sheep collagen. From 6 wk. the hexamethylenediisocyanate-tanned dermal sheep collagen implant was replaced by rat connective tissue, which was subsequently also degraded. After 15 wk. the presence of basophil-like foreign body multinucleated giant cells containing aluminium/silicon-crystalline accumulations still persisted. These phenomena were related to the specific nature of the material used and suggest cytotoxicity. They emphasize the need for detailed evaluation at the ultrastructural level of newly developed biomaterials before they can be used for medical applications. Various collagen-based biomaterials have found applications in the biomedical fieldlm3. Interactions between such biomaterials and tissue have been extensively described4-6. However, these reports predominantly concern light microscopy evaluations. In our opinion, more detailed knowledge of the cellular events is needed for a better understanding and further improvement of the function of collagen-based biomaterials. In this study, we used hexamethylenediisocyanate-tanned dermal sheep collagen (HDSC), which was subcutaneously implanted in rats. The material is successfully Correspondence to Dr P.B. van Wachem @ 1991 Butterworth-Heinemann Ltd. 0142-9612/91/020215-09 used as a biological wound dressing'. It was tested in rabbits both after intramuscular implantation of small pieces' and after intracutaneous injections of extracts9 in accordance with US Pharmacopeia XXI (1985). The light microscopy evaluation of the intramuscular implantation test showed a very slight toxic reaction. No adverse reactions related to the material were observed in the intracutaneous injection test. Referring to the very slight toxic reaction observed in the intramuscular implantation test, it was the aim of this study to evaluate the degradation of HDSC in detail using transmission electron microscopy (TEM). . The material was processed from sheep skin, which was depilated, immersed in a lime-sodium sulphide solution for removal of the epidermis and purified with proteolytic enzymes7. The skin was then split with an industrial band-knife splitting machine to obtain the dermal layer. This layer was then tanned with HMDIC (Desmodur@ obtained from Bayer, Germany). Discs with a diameter of 8 mm were punched from HDSC. The weight of the discs varied from 15 to 30 mg. Discs were sterilized by gamma irradiation (2.5 Mrad, Gammaster, Ede, The Netherlands). Implantations. A0 rats of approximately 3 month of age Si were used. The rats were ether anaesthesized, their backs I were shaved and their skins disinfected with ethanol. Two midline incisions were made. Subcutaneous pockets were made with surgical scissors at the right and left sides of each incision. Four HDSC discs per rat were implanted in the pockets at a distance of about 1 cm from the incisions.