Collagen-based Biomaterials

Ramshaw, John A. M.; Werkmeister, Jerome A.; Glattauer, Veronica

doi:10.1080/02648725.1996.10647934

Cited by 153 publications

(120 citation statements)

References 162 publications

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“…2) lack of solubility was more of an issue, with possible aggregation associated with disulphide interchange between individual molecules. For the V-(CL) [1][2][3][4] cc series, the longest construct V-(CL) 4 cc was too insoluble for a reliable T m determination; after the V-domain was removed the (CL) 4 cc sample was too insoluble to allow any T m determination.…”

Section: Circular Dichroism (Cd) Spectroscopymentioning

confidence: 99%

“…For the V-(CL) [1][2][3][4] series, the longest construct V-(CL) 4 was very insoluble and not enough could be dissolved to get a good signal for a reliable T m determination; the www.landesbioscience.comsame was the case after the V-domain was removed. For all samples with the C-terminal Cys-Cys sequence (Fig.…”

Section: Circular Dichroism (Cd) Spectroscopymentioning

confidence: 99%

“…1,2 The most commonly used sources have been mammalian skin and tendon collagens, especially from bovines. However, as natural products, they can show batch to batch variability, which can affect the material properties.…”

Section: Introductionmentioning

confidence: 99%

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Preparation and characterization of monomers to tetramers of a collagen-like domain fromStreptococcus pyogenes

et al. 2014

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Abbreviations: V, non-collagenous N-terminal domain of the S. pyogenes collagen-like protein; CL, collagenous domain of the S.pyogenes collagen-like protein; VCL, full collagen-like protein structureThe collagen like domain Scl2 from Streptococcus pyogenes has been proposed as a potential biomedical material. It is non-cytotoxic and non-immunogenic and can be prepared in good yield in fermentation. The Scl2 collagen domain is about a quarter of the length, 234 residues, of the main collagen type, mammalian type I collagen (1014 residues) that is currently used in biomedical devices. In the present study we have made constructs comprising 1 to 4 copies of the Scl2 collagen domain, plus these same constructs with a CysCys sequence at the C-terminal, analogous to that found in mammalian type III collagens. The yields of these constructs were examined from 2 L fermentation studies. The yields of both series declined with increasing size. Circular dichroism showed that the addition of further collagen domains did not lead to a change in the melting temperature compared to the monomer domain. Addition of the CysCys sequence led to a small additional stabilization of about 2-3 C for the monomer construct when the folding (V) domain was present.

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Section: Circular Dichroism (Cd) Spectroscopymentioning

confidence: 99%

Section: Circular Dichroism (Cd) Spectroscopymentioning

confidence: 99%

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Preparation and characterization of monomers to tetramers of a collagen-like domain fromStreptococcus pyogenes

et al. 2014

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“…Its high natural abundance and intrinsic plasticity have spurred the development of collagen as a biomaterial (1,2). The most common source of clinical collagen is now Bos taurus, the domestic cow.…”

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confidence: 99%

Self-assembly of synthetic collagen triple helices

Kotch

Raines

2006

Proc. Natl. Acad. Sci. U.S.A.

281

232

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Collagen is the most abundant protein in animals and the major component of connective tissues. Although collagen isolated from natural sources has long served as the basis for some biomaterials, natural collagen is difficult to modify and can engender pathogenic and immunological side effects. Collagen comprises a helix of three strands. Triple helices derived from synthetic peptides are much shorter (<10 nm) than natural collagen (Ϸ300 nm), limiting their utility. Here, we describe the synthesis of short collagen fragments in which the three strands are held in a staggered array by disulfide bonds. Data from CD spectroscopy, dynamic light scattering, analytical ultracentrifugation, atomic force microscopy, and transmission electron microscopy indicate that these ''sticky-ended'' fragments self-assemble via intermolecular triple-helix formation. The resulting fibrils resemble natural collagen, and some are longer (>400 nm) than any known collagen. We anticipate that our self-assembly strategy can provide synthetic collagen-mimetic materials for a variety of applications.biomaterial ͉ coiled-coil ͉ nanotechnology ͉ cystine knot ͉ peptide C ollagen constitutes one-third of the human proteome, including three-quarters of the dry weight of human skin. Its high natural abundance and intrinsic plasticity have spurred the development of collagen as a biomaterial (1, 2). The most common source of clinical collagen is now Bos taurus, the domestic cow. Unfortunately, bovine collagen can illicit deleterious pathological and immunological effects when transplanted into humans (3-5). Moreover, the preparation of enriched solutions of natural collagen is problematic (6), and its sitespecific covalent modification is not feasible. We suspected that synthetic chemistry could offer a solution to these problems.The quaternary structure of collagen comprises three strands that wrap around one another to form a triple helix (7). Each strand has the repeating sequence XaaYaaGly, with the most abundant triplet being ProHypGly [Hyp ϭ (2 S,4R)-4-hydroxyproline] (8). The folding of (XaaYaaGly) nՅ10 peptides into blunt-ended triple helices has been investigated thoroughly (7). Although such triple helices are biomaterial candidates (9-12), they are limited to the length of a synthetic peptide (Ͻ10 nm), which is much shorter than natural collagen (Ϸ300 nm). The polymerization of (XaaYaaGly) 10 peptides has afforded long strands that adopt triple-helical structure but have high polydispersity (13).Molecular self-assembly underlies the ''bottom-up'' approach to macromolecular design, wherein a desirable structure forms spontaneously through noncovalent interactions (14, 15). Selfassembling peptides and proteins have been designed to serve as materials for biological and nanotechnological applications (16,17). Using the self-assembly approach, Woolfson and coworkers (18,19) have produced fibers with a design based on a dimeric coiled-coil structure. Likewise, fibrous peptides based on the natural protein elastin (20) and de novo building b...

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“…It helps in the migration of endothelial cells, activation of clotting factors, formation of fibroblats and also plays a vital role in the appearance of the final scar. Collagen also plays a major role in wound healing 39 . The matrix can be impregnated with a drug entity, thus acting as a reservoir for drug delivery.…”

Section: Semi-permeable Adhesive Film Dressingsmentioning

confidence: 99%

Advanced Trends in Treatment of Wounds

Miranda

Ganga

2016

Current Science

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There are a wide variety of dressing techniques available for the management of both acute and chronic wounds. The primary objective in both the cases is to achieve a healed wound. An ideal dressing material should accelerate wound healing and reduce loss of necessary fluids from the wound, and also help minimize pain and infection. The present trend is to promote the concept of moist wound healing. This article emphasizes on the importance of assessment of the wound, the volume of drainage fluid, amount of damage, presence of infection and location of wound for optimal wound healing.

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Collagen-based Biomaterials

Cited by 153 publications

References 162 publications

Preparation and characterization of monomers to tetramers of a collagen-like domain fromStreptococcus pyogenes

Preparation and characterization of monomers to tetramers of a collagen-like domain fromStreptococcus pyogenes

Self-assembly of synthetic collagen triple helices

Advanced Trends in Treatment of Wounds

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