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Abstract 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.
AbstractList 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.
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Snippet Protein adsorption to solids, nanomaterials, and biological surfaces is of central interest in many fields, including biomedicine, bioanalytical chemistry,...
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SubjectTerms adsorption
alpha-synuclein
amyloid fibrils
amyloidogenic proteins
Biochemistry
Biology, life sciences
charge displacement
concentration jump
conformational flexibility
conformational transition
Cu+-ATPase
electrogenicity
EPR spectroscopy
gold nanoparticles
ion translocation
lipid membranes
Mathematics and Science
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
Reference, Information and Interdisciplinary subjects
Research and information: general
sarcoplasmic reticulum Ca2+-ATPase
solid supported membrane
spin label extrinsic probes
supramolecular assembly
surface-immobilized protein
Tempol
β2-microglobulin
Title Protein Adsorption and Conformational Changes
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