Insights into a Protein-Nanoparticle System by Paramagnetic Perturbation NMR Spectroscopy.
Molecules
; 25(21)2020 Nov 07.
Article
en En
| MEDLINE
| ID: mdl-33171781
ABSTRACT
BACKGROUND:
The interaction between proteins and nanoparticles is a very relevant subject because of the potential applications in medicine and material science in general. Further interest derives from the amyloidogenic character of the considered protein, ß2-microglobulin (ß2m), which may be regarded as a paradigmatic system for possible therapeutic strategies. Previous evidence showed in fact that gold nanoparticles (AuNPs) are able to inhibit ß2m fibril formation in vitro.METHODS:
NMR (Nuclear Magnetic Resonance) and ESR (Electron Spin Resonance) spectroscopy are employed to characterize the paramagnetic perturbation of the extrinsic nitroxide probe Tempol on ß2m in the absence and presence of AuNPs to determine the surface accessibility properties and the occurrence of chemical or conformational exchange, based on measurements conducted under magnetization equilibrium and non-equilibrium conditions.RESULTS:
The nitroxide perturbation analysis successfully identifies the protein regions where protein-protein or protein-AuNPs interactions hinder accessibility or/and establish exchange contacts. These information give interesting clues to recognize the fibrillation interface of ß2m and hypothesize a mechanism for AuNPs fibrillogenesis inhibition.CONCLUSIONS:
The presented approach can be advantageously applied to the characterization of the interface in protein-protein and protein-nanoparticles interactions.Palabras clave
Texto completo:
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Bases de datos:
MEDLINE
Asunto principal:
Espectroscopía de Resonancia Magnética
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Proteínas
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Microglobulina beta-2
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Nanopartículas
Idioma:
En
Revista:
Molecules
Asunto de la revista:
BIOLOGIA
Año:
2020
Tipo del documento:
Article