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Interaction of aflatoxin B1 with some biologically important substances
Zeitschrift Fur Lebensmittel-Untersuchung Und -Forschung
|April 28, 1976
Summary
Aflatoxin B1 interacts with biological molecules like DNA and proteins. Spectrophotometry and fluorimetry revealed that aflatoxin B1 alters UV absorption and quenches fluorescence in substances including tryptophan, RNA, and bovine-serum albumin.
Area of Science:
- Biochemistry
- Molecular Biology
- Toxicology
Background:
- Aflatoxin B1 is a toxic metabolite with potential biological interactions.
- Understanding these interactions is crucial for assessing its toxicological impact.
Purpose of the Study:
- To investigate the interaction of aflatoxin B1 with biologically significant molecules.
- To characterize the binding and effects of aflatoxin B1 on these substances.
Main Methods:
- Spectrophotometric techniques were employed to measure changes in ultra-violet absorption.
- Fluorimetric methods, including fluorescence polarization, were used to assess fluorescence quenching and binding affinity.
Main Results:
- Aflatoxin B1 altered the ultra-violet absorption spectra of tryptophan, adenosine, RNA, and DNA.
- It quenched the fluorescence of amino acids, purine and pyrimidine derivatives, bovine-serum albumin, and DNA.
- Fluorescence polarization indicated a stronger interaction between aflatoxin B1 and bovine-serum albumin compared to DNA.
Conclusions:
- Aflatoxin B1 exhibits significant interactions with various biomolecules.
- The binding affinity varies, with stronger interactions observed with bovine-serum albumin than DNA.
- These findings contribute to understanding the molecular mechanisms of aflatoxin B1 toxicity.