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Research article

Clinical Microbiology and Biomedical Sciences

Synthetic Coprisin Analog Peptide, D-CopA3 has Antimicrobial Activity and Pro-Apoptotic Effects in Human Leukemia Cells

Soon-ja Kim 1, In-Woo Kim 1, Yong-Nam Kwon 1, Eun-Young Yun 1 and Jae-Sam Hwang 1*

Department of Agricultural Biology, National Academy of Agricultural Science, RDA, Suwon 441-853 South Korea

Received: October 21, 2011; Accepted: October 31, 2011

J. Microbiol. Biotechnol. 2012; 22(2): 264-269

Published February 28, 2012 https://doi.org/10.4014/jmb.1110.10071

Copyright © The Korean Society for Microbiology and Biotechnology.

Abstract

Recently, we reported that the synthetic Coprisin analog peptide 9-mer dimer CopA3 (consisted of all-L amino acid sequence) was designed based on a defensin-like peptide, Coprisin isolated from Copris tripartitus. The 9-mer dimer CopA3 (L-CopA3) had antibacterial activity and induced apoptosis in human leukemia cells via a caspase-independent pathway. In this study, all of amino acid sequences of LCopA3 were modified to all D-form amino acids (DCopA3) to develop a more effective antimicrobial peptide. We investigated whether D-CopA3 had antimicrobial activities against pathogenic microorganisms and proapoptotic effects in human leukemia cells (U937, Jurkat, and AML-2). The synthetic peptide D-CopA3 had antimicrobial activities against various pathogenic bacteria and yeast fungus with MIC values in the 4~64 μM range. Moreover, D-CopA3 caused cell growth inhibition, and increased the chromosomal DNA fragmentation and the expression of inflammatory cytokines, TNF-α and IL1-β, transcripts in human leukemia cells. The all-D amino acid peptide DCopA3 proved as effective as the L-CopA3 reported previously. These results provide the basis for developing D-CopA3 as a new antibiotic peptide.

Keywords

Coprisin analog peptide D-CopA3, antimicrobial peptide, defensin, antimicrobial activity, apoptosis

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Article

Research article

J. Microbiol. Biotechnol. 2012; 22(2): 264-269

Published online February 28, 2012 https://doi.org/10.4014/jmb.1110.10071

Copyright © The Korean Society for Microbiology and Biotechnology.

Synthetic Coprisin Analog Peptide, D-CopA3 has Antimicrobial Activity and Pro-Apoptotic Effects in Human Leukemia Cells

Soon-ja Kim 1, In-Woo Kim 1, Yong-Nam Kwon 1, Eun-Young Yun 1 and Jae-Sam Hwang 1*

Department of Agricultural Biology, National Academy of Agricultural Science, RDA, Suwon 441-853 South Korea

Received: October 21, 2011; Accepted: October 31, 2011

Abstract

Recently, we reported that the synthetic Coprisin analog
peptide 9-mer dimer CopA3 (consisted of all-L amino acid
sequence) was designed based on a defensin-like peptide,
Coprisin isolated from Copris tripartitus. The 9-mer dimer
CopA3 (L-CopA3) had antibacterial activity and induced
apoptosis in human leukemia cells via a caspase-independent
pathway. In this study, all of amino acid sequences of LCopA3
were modified to all D-form amino acids (DCopA3)
to develop a more effective antimicrobial peptide.
We investigated whether D-CopA3 had antimicrobial
activities against pathogenic microorganisms and proapoptotic
effects in human leukemia cells (U937, Jurkat, and
AML-2). The synthetic peptide D-CopA3 had antimicrobial
activities against various pathogenic bacteria and yeast
fungus with MIC values in the 4~64 μM range. Moreover,
D-CopA3 caused cell growth inhibition, and increased the
chromosomal DNA fragmentation and the expression of
inflammatory cytokines, TNF-α and IL1-β, transcripts in
human leukemia cells. The all-D amino acid peptide DCopA3
proved as effective as the L-CopA3 reported
previously. These results provide the basis for developing
D-CopA3 as a new antibiotic peptide.

Keywords: Coprisin analog peptide D-CopA3, antimicrobial peptide, defensin, antimicrobial activity, apoptosis