Article
Version 2
Preserved in Portico This version is not peer-reviewed
The Discovery of Synthetic Proteolytic Peptide
Version 1
: Received: 10 January 2018 / Approved: 12 January 2018 / Online: 12 January 2018 (05:29:13 CET)
Version 2 : Received: 17 January 2018 / Approved: 17 January 2018 / Online: 17 January 2018 (07:27:30 CET)
Version 2 : Received: 17 January 2018 / Approved: 17 January 2018 / Online: 17 January 2018 (07:27:30 CET)
How to cite: Nakamura, R.; Konishi, M.; Taniguchi, M.; Hatakawa, Y.; Akizawa, T. The Discovery of Synthetic Proteolytic Peptide. Preprints 2018, 2018010106. https://doi.org/10.20944/preprints201801.0106.v2 Nakamura, R.; Konishi, M.; Taniguchi, M.; Hatakawa, Y.; Akizawa, T. The Discovery of Synthetic Proteolytic Peptide. Preprints 2018, 2018010106. https://doi.org/10.20944/preprints201801.0106.v2
Abstract
After screening nearly 1000 synthetic peptides, a synthetic peptide termed JAL-AK22 (KYEGHWYPEKPYKGSGFRCIHI) derived from the BoxA domain in Tob1 protein was found to activate both unfolded and folded proMMP-7. In addition, JAL-AK22 showed auto-proteolytic activity. Interestingly, the smaller derivative of JAL-AK22 termed JAL-TA9 (YKGSGFRMI) also possessed auto-proteolytic activity and cleaved 2 fragment peptides (MMP18-33 and MMP18-40) derived from the prodomain of proMMP-7 under physiological conditions. These proteolytic activities were inhibited by AEBSF, a serine protease inhibitor. Our results demonstrate that a small synthetic peptide consisting of only 9 amino acids has serine protease-like activity and activates proMMP-7 by cleaving the prodomain region. We thus propose calling small peptides possessing with protease-like activity Catalytides (catalytic peptides). We expect that our findings will stimulate the development of novel Catalytides and related applications.
Keywords
catalytide; serine protease-like peptide; Tob1
Subject
Chemistry and Materials Science, Analytical Chemistry
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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