Premium
Specific Interaction Sites Determine Differential Adsorption of Protein Structural Isomers on Nanoparticle Surfaces
Author(s) -
Bortot Andrea,
Zanzoni Serena,
D'Onofrio Mariapina,
Assfalg Michael
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201705994
Subject(s) - chemistry , nanoparticle , covalent bond , adsorption , paramagnetism , protein–protein interaction , nuclear magnetic resonance spectroscopy , molecular dynamics , affinities , binding affinities , biophysics , crystallography , combinatorial chemistry , nanotechnology , computational chemistry , stereochemistry , materials science , biochemistry , organic chemistry , biology , physics , quantum mechanics , receptor
In biological systems, nanoparticles (NPs) elicit bioactivity upon interaction with proteins. As a result of post‐translational modification, proteins occur in a variety of alternative covalent forms, including structural isomers, which present unique molecular surfaces. We aimed at a detailed description of the recognition of protein isomeric species by NP surfaces. The transient adsorption of isomeric ubiquitin (Ub) dimers by NPs was investigated by solution NMR spectroscopy. Lys63‐ and Lys48‐linked Ub 2 were adsorbed by large anionic NPs with different affinities, whereas the binding strength was similar in the cases of smaller particles. After the incorporation of paramagnetic tags into NPs, the observed site‐resolved paramagnetic footprints provided a high‐resolution map of the different protein surfaces binding to NPs. The approach described could be extended to further protein isoforms and more specialized NP systems to allow better control of the interactions between NPs and protein targets.