New Insights into the Toxicity of n-Butanol to Trypsin: Spectroscopic and Molecular Docking Descriptions

Area of Science:

• Biochemistry
• Environmental Chemistry
• Molecular Biology

Background:

• n-Butanol is a widely used chemical with environmental persistence.
• Its residues can interact with biological molecules like trypsin.
• Understanding these interactions is crucial for environmental and biochemical studies.

Purpose of the Study:

• To investigate the complex formation between n-butanol and trypsin.
• To elucidate the conformational and functional changes induced by n-butanol.
• To determine the binding site and forces involved in the interaction.

Main Methods:

• Spectroscopic techniques (fluorescence, UV-visible absorption, synchronous fluorescence)
• Molecular docking and modeling
• Enzyme activity assays

Main Results:

• n-Butanol forms a complex with trypsin, affecting tryptophan fluorescence.
• Low n-butanol concentrations minimally impact trypsin conformation; high concentrations cause denaturation.
• Molecular modeling identified binding sites and forces, corroborating spectroscopic data.
• Enzyme activity assays demonstrated a dose-dependent response.

Conclusions:

• n-Butanol interacts with trypsin, leading to concentration-dependent conformational and functional alterations.
• The study provides insights into the molecular mechanisms of n-butanol toxicity.
• Findings are relevant for assessing the environmental impact of n-butanol on biological systems.