Preprint Article Version 2 This version is not peer-reviewed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)

How to cite: Nakamura, R.; Konishi, M.; Taniguchi, M.; Hatakawa, Y.; Akizawa, T. The Discovery of Synthetic Proteolytic Peptide. Preprints 2018, 2018010106 (doi: 10.20944/preprints201801.0106.v2). Nakamura, R.; Konishi, M.; Taniguchi, M.; Hatakawa, Y.; Akizawa, T. The Discovery of Synthetic Proteolytic Peptide. Preprints 2018, 2018010106 (doi: 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.

Subject Areas

catalytide; serine protease-like peptide; Tob1

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