| Literature DB >> 25482084 |
Yong Y Peng1, Violet Stoichevska, Linda Howell, Soren Madsen, Jerome A Werkmeister, Geoff J Dumsday, John A M Ramshaw.
Abstract
The 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.Entities:
Keywords: CL, collagenous domain of the S. pyogenes collagen-like protein; V, non-collagenous N-terminal domain of the S. pyogenes collagen-like protein; VCL, full collagen-like protein structure; collagen; fermentation; melting temperature; protein polymers; recombinant
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Year: 2014 PMID: 25482084 PMCID: PMC4601231 DOI: 10.4161/21655979.2014.969168
Source DB: PubMed Journal: Bioengineered ISSN: 2165-5979 Impact factor: 3.269