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Interchain disulfide bonds in crotamine self-association.

A M Teno¹, C A Vieira, M M Santoro

¹Departamento de Química Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Brasil.

Journal of Biochemistry

|June 1, 1990

Summary

Southern Brazilian rattlesnake venom contains crotamine, a neurotoxic protein. This protein exists as a dimer of two polypeptide chains, which can bind additional subunits.

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Area of Science:

Biochemistry
Toxicology
Molecular Biology

Background:

Crotamine is a basic neurotoxic protein found in the venom of the Southern Brazilian rattlesnake (Crotalus durissus terrificus).
Understanding the molecular structure of toxins is crucial for developing antivenoms and therapeutic agents.

Purpose of the Study:

To elucidate the molecular structure and quaternary organization of crotamine.
To investigate the aggregation state and subunit composition of crotamine.

Main Methods:

Isolation of crotamine by gel filtration.
Electrophoretic analysis using PAGE and SDS-PAGE under various conditions (pH, gel concentration, urea).
Molecular weight determination via SDS-PAGE and ultracentrifugal analysis.
Isolation and characterization of crotamine components using preparative PAGE.

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Main Results:

Native crotamine (NC) exhibited a molecular weight of 9,000-10,000 Da, while reduced and carboxymethylated crotamine (RCC) showed a molecular weight of 4,500-5,000 Da.
Electrophoretic analysis revealed that crotamine can form a dimer (9,760 Da) composed of two identical polypeptide chains linked by disulfide bonds.
Further analysis indicated the binding of additional subunits (4,880 Da each) to the dimeric structure.

Conclusions:

Crotamine exists as a dimeric structure with disulfide cross-linkages between identical polypeptide chains.
The dimeric crotamine structure appears to covalently bind additional subunits, contributing to its overall molecular complexity.
These findings provide insights into the structural basis of crotamine's neurotoxicity and potential for therapeutic applications.