TY - BOOK ID - 124998091 TI - Protein Adsorption and Conformational Changes PY - 2022 PB - Basel MDPI - Multidisciplinary Digital Publishing Institute DB - UniCat KW - Research & information: general KW - Biology, life sciences KW - Biochemistry KW - sarcoplasmic reticulum Ca2+-ATPase KW - Cu+-ATPase KW - phospholipid flippase KW - charge displacement KW - concentration jump KW - solid supported membrane KW - conformational transition KW - electrogenicity KW - ion translocation KW - phospholipid flipping KW - protein-nanoparticle interactions KW - protein NMR KW - amyloidogenic proteins KW - nitroxide paramagnetic perturbation KW - spin label extrinsic probes KW - Tempol KW - β2-microglobulin KW - protein conformation KW - protein-surface association KW - lipid membranes KW - surface-immobilized protein KW - EPR spectroscopy KW - alpha-synuclein KW - amyloid fibrils KW - conformational flexibility KW - protein adsorption KW - protein aggregation KW - nano-bio interface KW - nanocomposite KW - nanoparticles KW - supramolecular assembly KW - NMR spectroscopy KW - gold nanoparticles KW - PEGylation KW - adsorption KW - passivation KW - n/a UR - https://www.unicat.be/uniCat?func=search&query=sysid:124998091 AB - 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. ER -