Adsorption of plasma protein human serum albumin on surface functionalized multi-walled carbon nanotubes: Insights into binding interactions and effects on protein fibrillation
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View abstract on PubMed
Summary
This summary is machine-generated.This study investigated human serum albumin (HSA) interactions with functionalized carbon nanotubes (CNTs). Pristine CNTs showed higher adsorption, while functionalized CNTs demonstrated anti-fibrillation activity, inhibiting protein aggregation.
Area Of Science
- Biomaterials Science
- Nanotechnology
- Biochemistry
Background
- Carbon nanotubes (CNTs) show promise in biomedical applications.
- Understanding protein-CNT interactions and nanotoxicity is crucial.
- Human serum albumin (HSA) interactions with CNTs are not well-studied.
Purpose Of The Study
- To investigate HSA adsorption onto functionalized multi-walled carbon nanotubes (MWCNTs).
- To analyze binding parameters and anti-fibrillation activity of MWCNT-HSA interactions.
- To assess the impact of CNT surface functionalization on protein behavior.
Main Methods
- Experimentally studied HSA adsorption on pristine (p-MWCNTs), 1,2-propanediol (MWCNTs-OH), and cysteamine (MWCNTs-SH) functionalized MWCNTs.
- Utilized Isothermal Titration Calorimetry (ITC) for binding analysis.
- Assessed anti-fibrillation activity using Thioflavin T (ThT), Congo Red (CR), circular dichroism (CD), and microscopy.
Main Results
- Adsorption capacity order: p-MWCNTs > MWCNTs-SH > MWCNTs-OH.
- ITC revealed HSA forms complexes with MWCNTs-OH and MWCNTs-SH at specific binding sites.
- Surface functionalized MWCNTs exhibited anti-fibrillation activity, inhibiting HSA fibril formation.
Conclusions
- Surface functionalization significantly alters HSA adsorption and binding characteristics on MWCNTs.
- Functionalized MWCNTs show potential as inhibitors of protein fibrillation.
- Further research into CNT-protein interactions is warranted for biomedical applications.
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