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New Data from Jiangxi Agricultural University Illuminate Findings in Metalloendopeptidases (A quicker degradation rate is yielded by a novel kind of...

September 2, 2014



New Data from Jiangxi Agricultural University Illuminate Findings in Metalloendopeptidases (A quicker degradation rate is yielded by a novel kind of transgenic silk fibroin consisting of shortened silk fibroin heavy chains fused with matrix ...)

By a News Reporter-Staff News Editor at Life Science Weekly -- Current study results on Enzymes and Coenzymes have been published. According to news reporting originating in Nanchang, People's Republic of China, by NewsRx journalists, research stated, "Degradation performance of silk fibroin is an important property for its medical applications. Herein we constructed a shortened silk fibroin heavy chain protein fused with a matrix metalloproteinase cleavage site (SSFH-MMP) along with a glutathione S-transferase tag ahead."

The news reporters obtained a quote from the research from Jiangxi Agricultural University, "The digestion assay shows it can be cut by matrix metalloproteinase-2 (MMP-2) at its MMP cleavage site. Furthermore, we introduced the SSFH-MMP into silk fibroin by genetic modification of silkworms in order to increase the degradation rate of the silk fibroin. After acquisition of a race of transgenic silkworms with the coding sequence of the MMP cleavage site in their genomic DNA, we tested some properties of their silk fibroin designated TSF-MMP. The results show that the TSF-MMP has MMP cleavage sites and yields a quicker degradation rate during dilution in MMP-2 enzyme buffer or implantation into tumor tissues compared with that of normal silk fibroin."

According to the news reporters, the research concluded: "Moreover, the TSF-MMP is in vitro non-toxic to human bone marrow mesenchymal stem cells (hBM-MSCs) indicating that the TSF-MMP may become a biomaterial with a quicker degradation rate for its medical applications."

For more information on this research see: A quicker degradation rate is yielded by a novel kind of transgenic silk fibroin consisting of shortened silk fibroin heavy chains fused with matrix metalloproteinase cleavage sites. Journal of Materials Science-Materials in Medicine, 2014;25(8):1833-1842. Journal of Materials Science-Materials in Medicine can be contacted at: Springer, Van Godewijckstraat 30, 3311 Gz Dordrecht, Netherlands (see also Enzymes and Coenzymes).

Our news correspondents report that additional information may be obtained by contacting G.P. Huang, Jiangxi Agr Univ, Coll Sci, Nanchang 330045, Jiangxi, People's Republic of China. Additional authors for this research include D.F. Yang, C.F. Sun, J.P. Huang, K.P. Chen, C.X. Zhang, H.Q. Chen and Q. Yao.

Keywords for this news article include: Asia, Nanchang, Proteomics, Peptide Hydrolases, Enzymes and Coenzymes, Metalloendopeptidases, Matrix Metalloproteinases, People's Republic of China

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC


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Source: Life Science Weekly


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