Studies on lysozyme modifications induced by substituted p-benzoquinones

Area of Science:

• Biochemistry
• Protein Chemistry
• Chemical Biology

Background:

• Protein misfolding leads to dysfunction and toxicity, implicated in various diseases.
• Quinone-induced protein modifications are understudied despite their potential role in pathogenesis.

Purpose of the Study:

• To investigate lysozyme modifications induced by benzoquinones (BQs).
• To explore the impact of BQ substituents and reaction conditions on protein modification.
• To correlate electrochemical properties of BQs with their reactivity towards lysozyme.

Main Methods:

• Fluorescence spectroscopy (including anisotropy)
• UV-Vis spectroscopy
• SDS-PAGE
• Cyclic voltammetry

Main Results:

• All tested BQs modified lysozyme via adduct formation, oligomerization, aggregation, and fibril formation.
• Substituent effects on BQs influenced the extent and nature of lysozyme modification.
• Reaction conditions (concentration, pH, temperature, time) affected lysozyme modification by 1,4-benzoquinone.
• Quinone reduction potentials correlated with their observed reactivity towards lysozyme.

Conclusions:

• Benzoquinones are potent modifiers of lysozyme, inducing complex structural changes.
• Electrochemical properties can predict the reactivity of quinones in protein modification.
• This study highlights the significance of quinone-induced protein damage.