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 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.
Dipartimento di Biotecnologie, Università degli Studi di Verona, Strada Le Grazie 15, 37134 Verona, Italy.
Michael
M
Assfalg
Laboratorio NMR, Istituto per lo Studio delle Macromolecole, CNR, Via Bassini 15, 20133 Milano, Italy.
Laura
L
Ragona
Laboratorio NMR, Istituto per lo Studio delle Macromolecole, CNR, Via Bassini 15, 20133 Milano, Italy.
Katiuscia
K
Pagano
Dipartimento di Biotecnologie, Università degli Studi di Verona, Strada Le Grazie 15, 37134 Verona, Italy.
Mariapina
M
D'Onofrio
Dipartimento di Biotecnologie, Università degli Studi di Verona, Strada Le Grazie 15, 37134 Verona, Italy.
Serena
S
Zanzoni
Laboratorio NMR, Istituto per lo Studio delle Macromolecole, CNR, Via Bassini 15, 20133 Milano, Italy.
Simona
S
Tomaselli
Laboratorio NMR, Istituto per lo Studio delle Macromolecole, CNR, Via Bassini 15, 20133 Milano, Italy. Electronic address: henriette.molinari@univr.it.
Henriette
H
Molinari
D041961:Deuterium Exchange Measurement / Q000379:methods; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D053758:Nanoparticles / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012996:Solutions
D011506:Proteins; D012996:Solutions
Interaction; NMR; Nanoparticle; Protein