Vai al contenuto principale della pagina
| Autore: |
Assfalg Michael
|
| Titolo: |
Protein Adsorption and Conformational Changes
|
| Pubblicazione: | Basel, : MDPI - Multidisciplinary Digital Publishing Institute, 2022 |
| Descrizione fisica: | 1 online resource (100 p.) |
| Soggetto topico: | Biochemistry |
| Biology, life sciences | |
| Research & information: general | |
| Soggetto non controllato: | adsorption |
| alpha-synuclein | |
| amyloid fibrils | |
| amyloidogenic proteins | |
| charge displacement | |
| concentration jump | |
| conformational flexibility | |
| conformational transition | |
| Cu+-ATPase | |
| electrogenicity | |
| EPR spectroscopy | |
| gold nanoparticles | |
| ion translocation | |
| lipid membranes | |
| n/a | |
| nano-bio interface | |
| nanocomposite | |
| nanoparticles | |
| nitroxide paramagnetic perturbation | |
| NMR spectroscopy | |
| passivation | |
| PEGylation | |
| phospholipid flippase | |
| phospholipid flipping | |
| protein adsorption | |
| protein aggregation | |
| protein conformation | |
| protein NMR | |
| protein-nanoparticle interactions | |
| protein-surface association | |
| sarcoplasmic reticulum Ca2+-ATPase | |
| solid supported membrane | |
| spin label extrinsic probes | |
| supramolecular assembly | |
| surface-immobilized protein | |
| Tempol | |
| β2-microglobulin | |
| Persona (resp. second.): | AssfalgMichael |
| Sommario/riassunto: | Protein adsorption to solids, nanomaterials, and biological surfaces is of central interest in many fields, including biomedicine, bioanalytical chemistry, materials engineering, bio-nanotechnology, and basic biomolecular research. Although protein adsorption may sometimes occur with little consequence on molecular structure, interactions with surfaces frequently cause changes in local or global conformations and dynamics, perturbations to secondary structures or tertiary folds, eventually resulting in dramatically altered protein function. Importantly, surfaces may trigger protein misfolding and self-aggregation, or, conversely, promote protein structure formation. The use of nanoscale surfaces to remodel the conformational landscape and the aggregation pathways of amyloidogenic peptides and proteins has been proposed as a promising strategy against several severe human diseases. The rapid growth of applications and technological innovation which is based on or concerned with protein adsorption necessitates renewed efforts to provide molecular-level insights into adsorption-induced protein structural perturbations. In this Special Issue, we gathered the recent findings of experimental and computational investigations that contributed novel insights into protein adsorption with a focus on the structural and dynamic aspects of proteins. |
| Titolo autorizzato: | Protein Adsorption and Conformational Changes ![]() |
| Formato: | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione: | Inglese |
| Record Nr.: | 9910566466103321 |
| Lo trovi qui: | Univ. Federico II |
| Opac: | Controlla la disponibilità qui |