Bioengineered collagens

Ramshaw, John A. M.; Werkmeister, Jerome A.; Dumsday, Geoff

doi:10.4161/bioe.28791

Cited by 36 publications

(17 citation statements)

References 50 publications

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“…The use of genetically engineered microorganisms, animals and plants appears to be an alternative option for the production of recombinant human collagens that avoids problems related to batch‐to‐batch variability, interspecies transmission of disease and xenogeneic immune responses, all of which can be induced by animal extracted collagens . The rational of using microorganisms as means to produce recombinant collagen lays on the fact that evolutionary collagens and collagen‐like proteins existed in bacteria before they were present in multicellular organisms . Saccharomyces cerevisiae and Pichia pastoris yeasts were the first to be investigated, given that as eukaryotes, they are capable of glycosylation.…”

Section: Sources Of Collagenmentioning

confidence: 99%

The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development

et al. 2018

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Collagen is the oldest and most abundant extracellular matrix protein that has found many applications in food, cosmetic, pharmaceutical, and biomedical industries. First, an overview of the family of collagens and their respective structures, conformation, and biosynthesis is provided. The advances and shortfalls of various collagen preparations (e.g., mammalian/marine extracted collagen, cell‐produced collagens, recombinant collagens, and collagen‐like peptides) and crosslinking technologies (e.g., chemical, physical, and biological) are then critically discussed. Subsequently, an array of structural, thermal, mechanical, biochemical, and biological assays is examined, which are developed to analyze and characterize collagenous structures. Lastly, a comprehensive review is provided on how advances in engineering, chemistry, and biology have enabled the development of bioactive, 3D structures (e.g., tissue grafts, biomaterials, cell‐assembled tissue equivalents) that closely imitate native supramolecular assemblies and have the capacity to deliver in a localized and sustained manner viable cell populations and/or bioactive/therapeutic molecules. Clearly, collagens have a long history in both evolution and biotechnology and continue to offer both challenges and exciting opportunities in regenerative medicine as nature's biomaterial of choice.

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Section: Sources Of Collagenmentioning

confidence: 99%

The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development

et al. 2018

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“…[12][13] These non-animal, bacterial collagens share the same characteristic triple-helical structure that is found in animal collagens and several other animal proteins. [16][17][18] However, the Scl2 collagen domain is small, about a quarter of the length, 234 residues, 19 of the abundant, mammalian interstitial collagens; eg type I, type II and type III collagens, which are just over 1000 residues each. 20 In order to make a bacterial collagen that is comparable in length to the mammalian interstitial collagen a tetramer of the S. pyogenes CL domain would be required.…”

Section: Introductionmentioning

confidence: 99%

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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“…Consequently, in terms of sourcing, silk is less accessible unlike other natural materials such as collagens, which are abundant, however are at higher risk for an undesirable response upon implantation. Collagen has been associated with product impurities, disease transmission, and increased likelihood of bacterial infection …”

Section: Silkmentioning

confidence: 99%

“…Hydroxylation of the proline is a highly complex process requiring special enzymes. Therefore, in spite of its repetitive amino acid sequence, collagen cannot be produced by most expression systems due to its need for extensive post‐translational modification . In this respect, recombinant silk proteins could be considered more ready than recombinant collagen proteins.…”

Section: Silkmentioning

confidence: 99%

Biomedical Applications of Recombinant Silk‐Based Materials

Aigner

DeSimone

Scheibel³

2018

Advanced Materials

248

203

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Silk is mostly known as a luxurious textile, which originates from silkworms first cultivated in China. A deeper look into the variety of silk reveals that it can be used for much more, in nature and by humanity. For medical purposes, natural silks were recognized early as a potential biomaterial for surgical threads or wound dressings; however, as biomedical engineering advances, the demand for high-performance, naturally derived biomaterials becomes more pressing and stringent. A common problem of natural materials is their large batch-to-batch variation, the quantity available, their potentially high immunogenicity, and their fast biodegradation. Some of these common problems also apply to silk; therefore, recombinant approaches for producing silk proteins have been developed. There are several research groups which study and utilize various recombinantly produced silk proteins, and many of these have also investigated their products for biomedical applications. This review gives a critical overview over of the results for applications of recombinant silk proteins in biomedical engineering.

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Bioengineered collagens

Cited by 36 publications

References 50 publications

The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development

The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development

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

Biomedical Applications of Recombinant Silk‐Based Materials

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