119th General Meeting of the KCS

Type Poster Presentation
Area 생명화학
Room No. 포스터발표장
Time 4월 21일 (금요일) 13:00~14:30
Code BIO.P-304
Subject Identification of Mycobacterium tuberculosis Caseinolytic protease C1 (ClpC1) binding peptide and synthesis of ecumicin-CBP derivatives
Authors 정인필, 하나름, 김아루, 김상헌, 최재우, 윤문영*
한양대학교 화학과, Korea
Abstract Caseinolytic protease C1 (ClpC1) in Mycobacterium tuberculosis (MTB) is a general stress protein which belongs to the heat shock protein 100 (hsp100) family of molecular chaperones. ClpC1 is a promising target for the development of new anti-tuberculosis agent, since ClpC1 have been identified as having a role in protein homeostasis in MTB strains. Ecumicin ClpC1 is one of the potent inhibitor for MTB based on the activation of ClpC1. In this study, we identified the ClpC1 binding peptide (CBP) by phage display. Among the identified peptide, 2 peptides (CBP1 and CBP2) exhibited similar binding and activation property to ecumicin. In order to increase the inhibition and permeability to MTB, CBPs were linked with ecumicin by esterification of Diepoxy butane. The size of synthesized derivatives was measured by MALDI-TOF and estimated to approximate 2.6 kDa consisted of 1.5 kDa Ecumicin and 1.1 kDa CBP. The synthesized derivatives exhibited ClpC1 activation property and inhibition against protease activity of ClpC1/ClpP1, P2 complex. This research might provide an impetus for the development of a strong anti-tuberculosis agent targeting MTB ClpC1.
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