Carbohydrate-Dependent Hemolytic Activity of the Conjugate Composed of a C-Type Lectin, CEL-I, and an Amphiphilic α-Helical Peptide, 43-βAla2

• Published in: Bioscience, biotechnology, and biochemistry Vol. 63; no. 7; pp. 1312 - 1314
• Main Authors: HATAKEYAMA, Tomomitsu, KAMINE, Tetsuji, KONISHI, Yuko, KUWAHARA, Hiromiki, NIIDOME, Takuro, AOYAGI, Haruhiko
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.01.1999; Japan Society for Bioscience Biotechnology and Agrochemistry
• Subjects: amphiphilic α-helical peptide; Biological and medical sciences; Biotechnology; carbohydrate-binding; conjugation; Fundamental and applied biological sciences. Psychology; hemolysis; lectin; Methods. Procedures. Technologies; Protein engineering; Hemolysis; Lectin; Binding capacity; Holothuroidea; Peptides; Echinodermata; Carbohydrate; Conjugation; Invertebrata; Conjugated compound; Amphiphilic compound; Biological activity
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.63.1312

A lectin-cationic peptide conjugate, 4 3 -CEL-I, was prepared from an invertebrate C-type lectin, CEL-I, and an amphiphilic α-helical peptide, 4 3 -βAla 2 [Ac-(Leu-Ala-Arg-Leu) 3 -βAla 2 ]. 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 -βAla 2 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.