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Published on: May 10, 2016
Deciphering the Nature of Caffeic Acid to Inhibit the HSA Aggregation Induced by Glyoxal
Waseem Feeroze Bhat1, Azaj Ahmed2, Shabeena Abbass1
1Department of Biochemistry, University of Kashmir, Hazratbal Srinagar - 190006, India.
Background:
Under certain circumstances, the path for protein folding deviates and attains an alternative path forming misfolded states, which are the key precursors for protein aggregation. Protein aggregation is associated with variety of diseases and leads to the cytotoxicity. These protein aggregate related diseases have been untreated so far. However, extensive attempts have been applied to develop anti-aggregating agents as possible approaches to overcome protein aggregation. Different types of substances have been reported to halt or decrease the formation of ordered protein aggregates both in vitro and in vivo, such as polyphenols and metal ions.
Objective:
In the present study the in vitro aggregation of human serum albumin (HSA) by using a reactive dicarbonyl glyoxal has been investigated, simultaneously an attempt has been done to inhibit the glyoxal (GO) induced aggregation of (HSA) by caffeic acid (CA).
Methods:
Different methods have been employed to investigate the process, fluorescence spectroscopy, circular dichroism, cango red binding assay, thioflavin T dye binding, turbidimetric analysis, docking study and transmission electron microscopy.
Results:
Results have shown that elevated concentration of GO forms aggregates of HSA, and the activity of CA suggested the possibility of inhibiting the HSA aggregation at higher concentrations, and this compound was found to have an anti-aggregation property.
Conclusion:
The present study explained that micro molar concentrations of CA inhibits the aggregation of HSA and showed pronounced anti-aggregation effect at increasing concentrations in the presence of GO which is elevated in diabetic and hyperglycaemia conditions.
Insights
Caffeic acid (CA) inhibits glyoxal-induced aggregation of human serum albumin (HSA), a key factor in diseases. This study demonstrates CA
Area of Science:
- Biochemistry
- Molecular Biology
- Disease Pathogenesis
Background:
- Protein misfolding and aggregation are implicated in various diseases.
- Misfolded proteins can aggregate, leading to cytotoxicity and untreatable conditions.
- Developing anti-aggregation agents is crucial for therapeutic interventions.
Purpose of the Study:
- Investigate in vitro aggregation of human serum albumin (HSA) induced by glyoxal (GO).
- Evaluate the inhibitory effect of caffeic acid (CA) on GO-induced HSA aggregation.
Main Methods:
- Utilized fluorescence spectroscopy, circular dichroism, and Congo red binding assays.
- Employed thioflavin T dye binding, turbidimetric analysis, and transmission electron microscopy.
- Performed molecular docking studies to understand interactions.
Main Results:
- Glyoxal (GO) at elevated concentrations induced HSA aggregation.
- Caffeic acid (CA) demonstrated significant anti-aggregation properties.
- CA effectively inhibited GO-induced HSA aggregation in a concentration-dependent manner.
Conclusions:
- Micro-molar concentrations of CA inhibit HSA aggregation induced by GO.
- CA exhibits a pronounced anti-aggregation effect, particularly relevant for conditions like diabetes and hyperglycemia.
- CA is a potential therapeutic agent against protein aggregation-related diseases.
