Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/14428
Title: Antitumor effects, cell selectivity and structure-activity relationship of a novel antimicrobial peptide polybia-MPI
Authors: Wang, KR
Zhang, BZ
Zhang, W
Yan, JX
Li, J
Wang, R
Keywords: Analog
Antimicrobial peptide
Antitumor
Cell selectivity
Polybia-MPI
Issue Date: 2008
Publisher: Elsevier Science Inc
Source: Peptides, 2008, v. 29, no. 6, p. 963-968 How to cite?
Journal: Peptides 
Abstract: A novel antimicrobial peptide, polybia-MPI, was purified from the venom of the social wasp Polybia paulista. It has potent antimicrobial activity against both Gram-positive and Gram-negative bacteria, but causing no hemolysis to rat erythrocytes. To date, there is no report about its antitumor effects on any tumor cell lines. In this study we synthesized polybia-MPI and studied its antitumor efficacy and cell selectivity. Our results revealed that polybia-MPI exerts cytotoxic and antiproliferative efficacy by pore formation. It can selectively inhibit the proliferation of prostate and bladder cancer cells, but has lower cytotoxicity to normal murine fibroblasts. In addition, to investigate the structure-activity relationship of polybia-MPI, three analogs in which Leu 7, Ala 8 or Asp 9 replaced by l-Pro were designed and synthesized. l-Pro substitution of Leu 7 or Asp 9 significantly reduces the content of α-helix conformation, and l-Pro substitution of Ala 8 can disrupt the α-helix conformation thoroughly. The l-Pro substitution induces a significant reduction of antitumor activity, indicating that the α-helix conformation of polybia-MPI is important for its antitumor activity. In summary, polybia-MPI may offer a novel therapeutic strategy in the treatment of prostate cancer and bladder cancer, considering its relatively lower cytoxicity to normal cells.
URI: http://hdl.handle.net/10397/14428
DOI: 10.1016/j.peptides.2008.01.015
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