Bauhinia variegata var. variegata trypsin inhibitor: from isolation to potential medicinal applications

Biochem Biophys Res Commun. 2010 Jun 11;396(4):806-11. doi: 10.1016/j.bbrc.2010.04.140. Epub 2010 May 8.

Abstract

Here we report for the first time of a new Kunitz-type trypsin inhibitor (termed BvvTI) from seeds of the Camel's foot tree, Bauhinia variegata var. variegata. BvvTI shares the same reactive site residues (Arg, Ser) and exhibits a homology of N-terminal amino acid sequence to other Bauhinia protease inhibitors. The trypsin inhibitory activity (K(i), 0.1 x 10(-9)M) of BvvTI ranks the highest among them. Besides anti-HIV-1 reverse transcriptase activity, BvvTI could significantly inhibit the proliferation of nasopharyngeal cancer CNE-1 cells in a selective way. This may partially be contributed by its induction of cytokines and apoptotic bodies. These results unveil potential medicinal applications of BvvTI.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anti-HIV Agents / chemistry
  • Anti-HIV Agents / isolation & purification
  • Anti-HIV Agents / pharmacology*
  • Antineoplastic Agents* / chemistry
  • Antineoplastic Agents* / isolation & purification
  • Antineoplastic Agents* / pharmacology
  • Apoptosis
  • Bauhinia / metabolism*
  • Cell Line, Tumor
  • Cell Proliferation / drug effects
  • Cytokines / biosynthesis
  • HIV-1 / drug effects
  • HIV-1 / enzymology
  • Humans
  • Male
  • Mice
  • Mice, Inbred BALB C
  • Nasopharyngeal Neoplasms / immunology
  • Peptides* / chemistry
  • Peptides* / isolation & purification
  • Peptides* / pharmacology
  • Plant Proteins* / chemistry
  • Plant Proteins* / isolation & purification
  • Plant Proteins* / pharmacology
  • Protein Stability
  • Reverse Transcriptase Inhibitors / chemistry
  • Reverse Transcriptase Inhibitors / isolation & purification
  • Reverse Transcriptase Inhibitors / pharmacology

Substances

  • Anti-HIV Agents
  • Antineoplastic Agents
  • Cytokines
  • Kunitz-type protease inhibitor, plant
  • Peptides
  • Plant Proteins
  • Reverse Transcriptase Inhibitors