Abstract
Gradual deterioration of nerve structures essential for brain functions can occur due to neurodegenerative diseases. Many natural and synthetic compounds can boost or diminish this disease depending upon the structure and electronic features of the compound. We have synthesized three benzofuran molecules having neutral, electron-rich, and electron-deficient natures. They are allowed to interact with β-sheet enriched model protein β-lactoglobulin (β-lg). They are capable of strong interaction with protein through hydrophobic interactions. Such interactions of the compounds alter the β-sheet structure into β-turns and α-helix. This conformational transformation of the protein influenced an increase in the protein surface hydrophobicity (confirmed by ANS assay), which allowed the protein to interact with another protein with a similar structure. Thus, the benzofuran molecules influence the protein aggregation process, identified using Th T assay and AFM studies. In this process, the electron-rich molecule is more efficient than the electron-deficient molecule. Therefore, electron-rich benzofuran molecules can increase protein aggregation by increasing the protein surface hydrophobicity by changing its conformation.
Published Version
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