Prion like behavior of HSA-hydroxylated MWCNT interface

Area of Science:

• Biomedical Engineering
• Materials Science
• Biochemistry

Background:

• Carbon nanotubes (CNTs) possess unique properties with potential biomedical applications.
• Understanding protein-CNT interactions is crucial for assessing toxicological risks.
• Human serum albumin (HSA) is a key protein in the human body.

Purpose of the Study:

• To investigate the interaction between functionalized CNTs and HSA.
• To elucidate the structural changes in HSA upon interaction with CNTs.
• To assess the effect of CNTs on HSA amyloid fibril formation.

Main Methods:

• UV-Visible spectroscopy to detect ground state complex formation.
• Synchronous and 3D fluorescence spectroscopy to identify binding sites.
• Fourier Transform Infrared (FTIR) and FT-Raman spectroscopy for structural analysis.
• Circular Dichroism (CD) spectroscopy (far and near UV) to determine secondary structure changes.
• Microscopic evaluations to confirm fibril formation.

Main Results:

• Hyperchromicity and decreased fluorescence of HSA indicate complex formation with CNTs.
• Spectroscopic data suggest binding near Trp and Tyr residues.
• Alterations in alpha-helical structures and loss of secondary structure observed in HSA.
• CNTs promote the formation of HSA amyloid fibrils, showing increased beta-sheet structures.
• Evidence of CNT aggregation in the presence of HSA.

Conclusions:

• CNTs interact with HSA, causing significant structural modifications.
• CNTs promote HSA amyloid fibril formation, similar to prion protein behavior.
• The HSA fibril-CNT interface may play a role in amyloid-related disorders and toxic accumulation.