In Situ Investigation on the Protein Corona Formation of Quantum Dots by Using Fluorescence Resonance Energy Transfer.
Shaohua QuFangying SunZihan QiaoJuanmin LiLi ShangPublished in: Small (Weinheim an der Bergstrasse, Germany) (2020)
A fundamental understanding of nanoparticle-protein corona and its interactions with biological systems is essential for future application of engineered nanomaterials. In this work, fluorescence resonance energy transfer (FRET) is employed for studying the protein adsorption behavior of nanoparticles. The adsorption of human serum albumin (HSA) onto the surface of InP@ZnS quantum dots (QDs) with different chirality (d- and l-penicillamine) shows strong discernible differences in the binding behaviors including affinity and adsorption orientation that are obtained upon quantitative analysis of FRET data. Circular dichroism spectroscopy further confirms the differences in the conformational changes of HSA upon interaction with d- and l-chiral QD surfaces. Consequently, the formed protein corona on chiral surfaces may affect their following biological interactions, such as possible protein exchange with serum proteins plasma as well as cellular interactions. These results vividly illustrate the potential of the FRET method as a simple yet versatile platform for quantitatively investigating biological interactions of nanoparticles.
Keyphrases
- energy transfer
- quantum dots
- single molecule
- protein protein
- sensitive detection
- binding protein
- cystic fibrosis
- high throughput
- machine learning
- pseudomonas aeruginosa
- ionic liquid
- risk assessment
- aqueous solution
- molecular dynamics
- capillary electrophoresis
- transcription factor
- big data
- artificial intelligence
- candida albicans
- single cell