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- Title
Improvement of thermostability of recombinant collagen-like protein by incorporating a foldon sequence.
- Authors
Chunling Du; Mingqi Wang; Jinying Liu; Mingli Pan; Yurong Cai; Juming Yao
- Abstract
Collagen is a popular biomaterial in many specific biological interactions as well as a structural element. In this work, the recombinant collagen-like proteins were synthesized using Escherichia coli expression system. A foldon sequence, GYIPEAPRDGQAYVRKDGEWVLLSTFL, derived from the native T4 phage fibritin was incorporated at the C-terminal of collagen-like protein molecules to stabilize the triple helix formed in the proteins. The differential scanning calorimetry and thermogravimetric analysis measurements showed that the thermostability of the recombinant collagen-like proteins was significantly improved when compared with those without the foldon sequence at the C-terminal. Fourier transform infrared and scanning electron microscopy observations indicated that the collagen-like proteins forms the triple helix structure and prefer to aggregate as fibrils, same as the native collagen. Moreover, the mice fibroblasts L929 cells could attach and grew very well on the recombinant collage-like proteins. 3-(4,5-Dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide assay showed that the cell biocompatibility of collagen-like proteins produced in this work was even better than that of native collagen, suggesting that the collagen-like proteins may be a satisfactory candidate for the future applications as a biomaterial.
- Subjects
COLLAGEN; CONNECTIVE tissues; ADIPOSE tissues; BIOMEDICAL materials; BIOMEDICAL engineering; BIOMOLECULES; EXTRACELLULAR matrix proteins; ELECTRON microscopy; ESCHERICHIA coli
- Publication
Applied Microbiology & Biotechnology, 2008, Vol 79, Issue 2, p195
- ISSN
0175-7598
- Publication type
Article
- DOI
10.1007/s00253-008-1427-0