2016
DOI: 10.2174/1385272820666151102213025
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Modification of Collagen for Biomedical Applications: A Review of Physical and Chemical Methods

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Cited by 43 publications
(17 citation statements)
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“…Gelatin, being low in calories, is widely used in food, photographic, cosmetic, biomedical, pharmaceutical, and neutraceutical industries (Al‐Kahtani et al, ; Kumar, Chandra, Elavarasan, & Shamasundar, ; Sha et al, ; Yu et al, ). It has been reported that the global demand for gelatin is expected to reach 450.7 kt in 2018 (Huang et al, ), with around 98.5% is extracted from mammalian sources including pig skins, bovine hides, and beef bones, etc.…”
Section: Introductionmentioning
confidence: 99%
“…Gelatin, being low in calories, is widely used in food, photographic, cosmetic, biomedical, pharmaceutical, and neutraceutical industries (Al‐Kahtani et al, ; Kumar, Chandra, Elavarasan, & Shamasundar, ; Sha et al, ; Yu et al, ). It has been reported that the global demand for gelatin is expected to reach 450.7 kt in 2018 (Huang et al, ), with around 98.5% is extracted from mammalian sources including pig skins, bovine hides, and beef bones, etc.…”
Section: Introductionmentioning
confidence: 99%
“…The uterine horn, like the human Fallopian tube, is a moist tubal environment with dynamic fluid secretion and absorption and a virtual and corrugated lumen, requiring a conformable implant. An EDS-NHS crosslinked, porous collagen scaffold unlocked the functionalities of fluid absorption and resiliency to fill the uterine space without compaction of the porosity; these properties are a result of the covalent bonds formed through chemical crosslinking [10]. The conserved porosity was visible both under confocal microscopy (Figure 1A) and in situ (Figure 3B), validating that our structure is robust for this application.…”
Section: Discussionmentioning
confidence: 55%
“…Collagen, as the most abundant protein in mammals, has been extensively researched and applied in the fields of medicine, tissue engineering, cosmetics, and so on, owing to its advantages such as good biocompatibility, low antigenicity, and controlled biodegradability . Therefore, collagen has been widely accepted as a quite promising biomaterial, however, some defects, particularly, the low mechanical strength, poor thermal stability, and vulnerability to enzymatic degradation still cannot be overlooked, which significantly restricted the applications of collagen . Accordingly, many chemical modifiers such as glutaraldehyde (GTA) , carbodiimide , acylazide , genipin , plant tannins , polyepoxy compound , and dialdehyde compound derived from natural biomass have been employed on collagen in order to obtain ideal physicochemical performance and thus meet the requirements for in vivo and in vitro applications.…”
Section: Introductionmentioning
confidence: 99%
“…Of the various modifiers, carbodiimide could form a typical “zero‐length” cross‐linking between collagen molecules , and thus perfectly avoiding any extra cytotoxicity into the modified collagen. In addition, N‐hydroxysuccinimide (NHS) could assist the O‐acylisourea group in converting into the more stable NHS‐activated carboxylic acid group , enhancing the carbodiimide cross‐linking efficiency for collagen . It should be pointed out that, however, the carboxylic and amine groups were not easy to be cross‐linked each other by carbodiimide for their distance.…”
Section: Introductionmentioning
confidence: 99%