Sesquin, a potent defensin-like antimicrobial peptide from ground beans with inhibitory activities toward tumor cells and HIV-1 reverse transcriptase

• Published in: Peptides (New York, N.Y. : 1980) Vol. 26; no. 7; pp. 1120 - 1126
• Main Authors: Wong, Jack Ho, Ng, Tzi Bun
• Format: Journal Article
• Language: English
• Published: New York, NY Elsevier Inc 01.07.2005; Elsevier Science
• Subjects: Animals; Antifungal Agents - isolation & purification; Antifungal Agents - pharmacology; Antifungal peptides; Antineoplastic Agents, Phytogenic - isolation & purification; Antineoplastic Agents, Phytogenic - pharmacology; Bacillus megaterium; Bean; Biological and medical sciences; Botrytis cinerea; Defensins - isolation & purification; Defensins - pharmacology; Escherichia coli; Fabaceae - chemistry; Fundamental and applied biological sciences. Psychology; Fusarium oxysporum; HIV Reverse Transcriptase - antagonists & inhibitors; Human immunodeficiency virus 1; Humans; Isolation; Mice; Mycobacterium phlei; Mycosphaerella arachidicola; Proteus vulgaris; Reverse Transcriptase Inhibitors - isolation & purification; Reverse Transcriptase Inhibitors - pharmacology; Tumor Cells, Cultured; Vertebrates: endocrinology; Vigna; Vigna sesquipedalis; Isolation; Vigna sesquipedalis; Antifungal peptides; Bean; RNA-directed DNA polymerase; Peptides; Enzyme; Transferases; Retroviridae; Vigna; Lentivirus; Virus; Nucleotidyltransferases; Leguminosae; Dicotyledones; Angiospermae; Spermatophyta; Human immunodeficiency virus; Antibacterial agent; Defensin; Tumor cell
• ISSN: 0196-9781; 1873-5169
• DOI: 10.1016/j.peptides.2005.01.003

An antifungal peptide with a molecular mass around 7 kDa and an N-terminal sequence highly homologous to defensin was isolated from ground beans ( Vigna sesquipedalis cv. ‘Ground Bean’). The peptide was adsorbed on Affi-gel blue gel and on Mono S. It exerted an antifungal action on Botrytis cinerea, Fusarium oxysporum and Mycosphaerella arachidicola; and an antibacterial action on Escherichia coli B, Proteus vulgaris, Mycobacterium phlei and Bacillus megaterium. The antimicrobial activity was inhibited in presence of the 5 mM CaCl 2 and MgCl 2, but no inhibition was observed in 5 mM NaCl. The peptide exerted antiproliferative activity toward breast cancer (MCF-7) cells and leukemia M1 cells, this activity could not be inhibited by the ions mentioned above. It also exhibited some inhibitory activity toward human immunodeficiency virus-type 1 reverse transcriptase.