EFFECT OF GUANDINIUM SALTS ON THE TOXICITY OF BOTULINUM TOXIN

Abstract

The effect of guanidinium salts on the stability of botulinum toxin and the mechanisms through which denaturation by these salts occurs is described. Some salts are effective in reducing toxicity at low concentrations; in others, toxicity is retainedeven in saturated solution. The nature of the interaction is complex, involving more than a change in folding or conformation. The hypothesis that salt solutions with high thermodynamic water activity labilize the hydrogen-bonded structure of the protein is shown to be invalid. Also shown to be inapplicable is the hypothesis that a direct effect of the anion on the quanidinium cation leads to a reduction of its thermodynamic activity and ability to break hydrogen bonds. The protective mechanism appears to operate via binding of anions across clusters of cationic sites on the charged protein to preserve spatial configurations and charge distributions.

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Document Details

Document Type
Technical Report
Publication Date
Oct 01, 1963
Accession Number
AD0424666

Entities

People

  • David Stefanye
  • Edward J. Schantz
  • Leonard Sepro
  • Robert T. Iwamasa

Organizations

  • United States Army Biological Warfare Laboratories

Tags

DTIC Thesaurus Topics

  • Albumins
  • Amino Acids
  • Biological Laboratories
  • Chlorides
  • Coefficients
  • Elements
  • Fatty Acids
  • Fluorides
  • Free Energy
  • Hydrogen
  • Hydrogen Bonds
  • Laboratory Animals
  • Laboratory Equipment
  • Materials
  • New York
  • Potassium Compounds
  • United States

Fields of Study

  • Chemistry

Readers

  • Calculus or Mathematical Analysis
  • Molecular and Cellular Biochemistry