Carbohydrate-dependent hemolytic activity of the conjugate composed of a C-type lectin, CEL-I, and an amphiphilic alpha-helical peptide, 4(3)-beta Ala2

Biosci Biotechnol Biochem. 1999 Jul;63(7):1312-4. doi: 10.1271/bbb.63.1312.

Abstract

A lectin-cationic peptide conjugate, 4(3)-CEL-I, was prepared from an invertebrate C-type lectin, CEL-I, and an amphiphilic alpha-helical peptide, 4(3)-beta Ala2 [Ac-(Leu-Ala-Arg-Leu)3-beta Ala2]. When 4(3)-CEL-I was incubated with rabbit erythrocytes, hemolysis was observed, especially at basic pH. Inhibition experiment using some carbohydrates suggested that hemolytic activity of 4(3)-CEL-I was caused by the interaction between 4(3)-beta Ala2 portion in the conjugate and the lipid bilayer after binding to the carbohydrate chains on the cell surface by the lectin activity of CEL-I.

MeSH terms

  • Animals
  • Carbohydrate Metabolism*
  • Carbohydrates / chemistry
  • Electrophoresis, Polyacrylamide Gel
  • Erythrocytes / drug effects
  • Hemolysis / drug effects*
  • Hydrogen-Ion Concentration
  • In Vitro Techniques
  • Lectins / chemistry
  • Lectins / pharmacology*
  • Peptides
  • Proteins / chemistry
  • Proteins / pharmacology*
  • Rabbits
  • Sea Cucumbers / chemistry*
  • Sea Cucumbers / drug effects

Substances

  • Carbohydrates
  • Lectins
  • Peptides
  • Proteins
  • acetyl(leucyl-alanyl-arginyl-leucyl)3-beta-alanyl-beta-alanine