The study of transient protein–nanoparticle interactions by solution NMR spectroscopy

The rapid development of novel nanoscale materials for applications in biomedicine urges an improved characterization of the nanobio interfaces. Nanoparticles exhibit unique structures and properties, often different from the corresponding bulk materials, and the nature of their interactions with bi...

Full description

Saved in:
Bibliographic Details
Published in:Biochimica et biophysica acta. Proteins and proteomics 2016-01, Vol.1864 (1), p.102-114
Main Authors: Assfalg, Michael, Ragona, Laura, Pagano, Katiuscia, D'Onofrio, Mariapina, Zanzoni, Serena, Tomaselli, Simona, Molinari, Henriette
Format: Article
Language:English
Subjects:
Deuterium Exchange Measurement - methods
Interaction
Kinetics
Models, Chemical
Models, Molecular
Nanoparticle
Nanoparticles - chemistry
NMR
Nuclear Magnetic Resonance, Biomolecular - methods
Protein
Protein Binding
Protein Structure, Tertiary
Proteins - chemistry
Proteins - metabolism
Solutions
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The rapid development of novel nanoscale materials for applications in biomedicine urges an improved characterization of the nanobio interfaces. Nanoparticles exhibit unique structures and properties, often different from the corresponding bulk materials, and the nature of their interactions with biological systems remains poorly characterized. Solution NMR spectroscopy is a mature technique for the investigation of biomolecular structure, dynamics, and intermolecular associations, however its use in protein–nanoparticle interaction studies remains scarce and highly challenging, particularly due to unfavorable hydrodynamic properties of most nanoscale assemblies. Nonetheless, recent efforts demonstrated that a number of NMR observables, such as chemical shifts, signal intensities, amide exchange rates and relaxation parameters, together with newly designed saturation transfer experiments, could be successfully employed to characterize the orientation, structure and dynamics of proteins adsorbed onto nanoparticle surfaces. This review provides the first survey and critical assessment of the contributions from solution NMR spectroscopy to the study of transient interactions between proteins and both inorganic (gold, silver, and silica) and organic (polymer, carbon and lipid based) nanoparticles. This article is part of a Special Issue entitled: Physiological Enzymology and Protein Functions. •Critical assessment of the use of solution NMR spectroscopy to the study of biomolecule–nanoparticle interactions•Overview of organic and inorganic nanoparticle interactions•Future challenges in the field
ISSN:1570-9639
1878-1454
DOI:10.1016/j.bbapap.2015.04.024