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Coccinin, an antifungal peptide with antiproliferative and HIV-1 reverse transcriptase inhibitory activities from large scarlet runner beans.

Abstract
An antifungal peptide, designated coccinin, with a molecular mass of 7kDa and an N-terminal sequence resembling those of defensins, was purified from the seeds of large scarlet runner beans (Phaseolus coccineus cv. 'Major'). The peptide isolated was unadsorbed on DEAE-cellulose, and adsorbed on Affi-gel blue gel and Mono S. The peptide excerted antifungal activity on a number of fungal species including Botrytis cinerea, Coprinus comatus, Fusarium oxysporum, Mycosphaerella arachidicola, Physalospora piricola, and Rhizoctonia solani. It also inhibited proliferation in the leukemia cell lines HL60 and L1210, and reduced the activity of HIV-1 reverse transcriptase. However, it did not affect proliferation of mouse splenocytes.
AuthorsPatrick H K Ngai, T B Ng
JournalPeptides (Peptides) Vol. 25 Issue 12 Pg. 2063-8 (Dec 2004) ISSN: 0196-9781 [Print] United States
PMID15572193 (Publication Type: Comparative Study, Journal Article)
Chemical References
  • Antifungal Agents
  • Defensins
  • Mitogens
  • Peptides
  • Reverse Transcriptase Inhibitors
  • coccinin protein, Phaseolus coccineus
  • HIV Reverse Transcriptase
Topics
  • Amino Acid Sequence
  • Animals
  • Antifungal Agents (isolation & purification, pharmacology)
  • Cell Line, Tumor
  • Cell Proliferation (drug effects)
  • Defensins (pharmacology)
  • Fungi (drug effects)
  • HIV Reverse Transcriptase (antagonists & inhibitors)
  • HL-60 Cells
  • Humans
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Mitogens (pharmacology)
  • Mitosporic Fungi (drug effects)
  • Peptides (isolation & purification, pharmacology)
  • Phaseolus (chemistry)
  • Reverse Transcriptase Inhibitors (isolation & purification, pharmacology)
  • Spleen (cytology, drug effects)

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