Antigenicity and immunogenicity of collagen

Lynn, Andrew K.; Yannas, Ioannis V.; Bonfield, W.

doi:10.1002/jbm.b.30096

Cited by 684 publications

(481 citation statements)

References 114 publications

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“…The thermal stability of assembled 2 [melting temperature (T m )ϭ 47°C] was greater than that of assembled 1 (T m ϭ 26°C), as expected from the presence of Hyp residues in the Yaa position of 2 (29). These T m values exceed those expected for a triple helix of the tethered (ProYaaGly) 3 core of fragments 1 and 2, suggesting that the (ProYaaGly) 5 overhangs of 1 and 2 assemble to form (1) n and (2) n triple helices, respectively.…”

Section: Resultsmentioning

confidence: 66%

“…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)(4)(5). Moreover, the preparation of enriched solutions of natural collagen is problematic (6), and its sitespecific covalent modification is not feasible.…”

mentioning

confidence: 99%

“…1B). The intermolecular assembly of the overhanging (ProYaaGly) 5 segments yield collagen triple helices of unprecedented length.…”

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confidence: 99%

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Self-assembly of synthetic collagen triple helices

Kotch

Raines

2006

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

278

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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Section: Resultsmentioning

confidence: 66%

mentioning

confidence: 99%

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Self-assembly of synthetic collagen triple helices

Kotch

Raines

2006

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

278

232

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“…Thus, resorbable GBR membranes are more desirable. Bovine or porcine collagen has been used as a material for resorbable GBR membranes 7,[14][15][16][17][18][19] ; however, although collagen is a highly biocompatible major matrix protein, the risk of infection with known or unknown diseases from the source animals cannot be completely eliminated, because of the physicochemically mild collagen extraction procedure [20][21][22] . An unfavorable immune reaction to the heterogeneous protein, although rare, is another concern regarding this material.…”

Section: Introductionmentioning

confidence: 99%

Guided bone regeneration using a hydrophilic membrane made of unsintered hydroxyapatite and poly(L-lactic acid) in a rat bone-defect model

et al. 2018

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The effectiveness of a previously developed unsintered hydroxyapatite (uHA) and poly(L-lactic acid) (PLLA) hydrophilic membrane as a resorbable barrier for guided bone regeneration (GBR) was evaluated. Critical-size 8-mm diameter bone defects were surgically generated in the parietal bones of 24 12-week-old male Wistar rats, which were then divided into three groups in which either a uHA/ PLLA or a collagen membrane or no membrane (control) was placed onto the bone defect. Following sacrifice of the animals 2 or 4 weeks after surgery, bone defects were examined using microcomputed tomography and histological analysis. Bone mineral density, bone mineral content, and relative bone growth area values 2 or 4 weeks after surgery were highest in the uHA/PLLA group. Four weeks after surgery, the relative bone growth area in the uHA/PLLA group was larger than that in the collagen group. The resorbable uHA/PLLA membrane is thus potentially effective for GBR.

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“…34 Our initial studies with porcine ECMp in cocultures with complete human peripheral blood mononuclear cells (PBMCs) showed distinct effects on induced immune cell proliferation and secretion of proinflammatory cytokines in vitro. 35 However, the induction of potential responses by isolated subsets of immune cells has not yet been characterized in detail for porcine and bovine collagen I and elastin.…”

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confidence: 99%

Absence of Immune Responses with Xenogeneic Collagen and Elastin

Bayrak

Prüger

Stock

et al. 2013

Tissue Engineering Part A

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Novel tissue-engineering approaches for cardiovascular matrices based on xenogeneic extracellular matrix protein (ECMp) constituents require a detailed evaluation of their interaction with essential immune cell subsets playing a role in innate or adaptive immunity. Therefore, in this study, the effects of xenogeneic (porcine, bovine) collagen type I and elastin as the two main components of the heart valve ECM were analyzed in comparison to their human equivalents. First, their potential to induce maturation and cytokine secretion of human dendritic cells (DC) was tested by flow cytometry. Second, the influence on proliferation and cytokine release of purified human B and T cells was measured. We could demonstrate that xenogeneic collagen type I and elastin are not able to trigger the maturation of DC as verified by the lack of CD83 induction accompanied by a low tumor necrosis factor-a release. Moreover, both ECMp showed no effect on the proliferation and the interleukin-6 release of either unstimulated or prestimulated B cells. Additionally, anti-CD3-induced purified T cell proliferation and secretion of cytokines was not affected. All in vitro data verify the low immunogenicity of porcine and bovine collagen type I and elastin and favor their suitability for tissue-engineered scaffolds.

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Antigenicity and immunogenicity of collagen

Cited by 684 publications

References 114 publications

Self-assembly of synthetic collagen triple helices

Self-assembly of synthetic collagen triple helices

Guided bone regeneration using a hydrophilic membrane made of unsintered hydroxyapatite and poly(L-lactic acid) in a rat bone-defect model

Absence of Immune Responses with Xenogeneic Collagen and Elastin

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