Protein Adsorption and Conformational Changes
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 conseque...
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Format | eBook |
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Language | English |
Published |
Basel
MDPI - Multidisciplinary Digital Publishing Institute
2022
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Subjects | |
Online Access | Get full text |
ISBN | 9783036526911 9783036526904 3036526919 3036526900 |
DOI | 10.3390/books978-3-0365-2690-4 |
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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. |
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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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