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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.

Research & information: general --- Biology, life sciences --- Biochemistry --- sarcoplasmic reticulum Ca2+-ATPase --- Cu+-ATPase --- phospholipid flippase --- charge displacement --- concentration jump --- solid supported membrane --- conformational transition --- electrogenicity --- ion translocation --- phospholipid flipping --- protein-nanoparticle interactions --- protein NMR --- amyloidogenic proteins --- nitroxide paramagnetic perturbation --- spin label extrinsic probes --- Tempol --- β2-microglobulin --- protein conformation --- protein-surface association --- lipid membranes --- surface-immobilized protein --- EPR spectroscopy --- alpha-synuclein --- amyloid fibrils --- conformational flexibility --- protein adsorption --- protein aggregation --- nano-bio interface --- nanocomposite --- nanoparticles --- supramolecular assembly --- NMR spectroscopy --- gold nanoparticles --- PEGylation --- adsorption --- passivation --- sarcoplasmic reticulum Ca2+-ATPase --- Cu+-ATPase --- phospholipid flippase --- charge displacement --- concentration jump --- solid supported membrane --- conformational transition --- electrogenicity --- ion translocation --- phospholipid flipping --- protein-nanoparticle interactions --- protein NMR --- amyloidogenic proteins --- nitroxide paramagnetic perturbation --- spin label extrinsic probes --- Tempol --- β2-microglobulin --- protein conformation --- protein-surface association --- lipid membranes --- surface-immobilized protein --- EPR spectroscopy --- alpha-synuclein --- amyloid fibrils --- conformational flexibility --- protein adsorption --- protein aggregation --- nano-bio interface --- nanocomposite --- nanoparticles --- supramolecular assembly --- NMR spectroscopy --- gold nanoparticles --- PEGylation --- adsorption --- passivation

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Aberrant protein folding and self-assembly underlie over 30 human diseases called amyloidoses, for which currently there is no cure. The diseases range from tissue-specific to systemic and from genetic to sporadic. Some of the most devastating amyloidoses are those that affect the central nervous system (CNS), such as Alzheimer’s disease (AD), Parkinson’s disease (PD), prionoses (e.g., mad-cow disease), and amyotrophic lateral sclerosis (Lou Gehrig’s disease). In each disease, one or more proteins self-associate into toxic oligomers that disrupt cellular function and communication, and proceed to form insoluble amyloid aggregates characterized by fibrillar morphology and cross-β structure. The first decade of the 21st century has brought with it significant progress in our understanding of amyloid diseases, including the physiological and pathological processes involving each of the offending proteins. Important developments also provide now improved diagnoses of different amyloidoses and new approaches are being developed towards disease-modifying therapies. This book covers the current state-of-the-art knowledge on amyloidoses as a general phenomenon and offers detailed reviews of individual amyloid-forming proteins and specific diseases. Features: Coverage of the pathologic and pathogenic structures of amyloidogenic proteins from the pathological lesions to the evasive oligomers that are believed to be the main culprits. Detailed discussions of diseases of epidemic proportion, such as Alzheimer’s disease, Parkinson’s disease, and type-2 diabetes. Current reviews of multiple diseases, including amyotrophic lateral sclerosis, prionoses, expanded polyglutamine diseases, dialysis-related amyloidosis, and transthyretin-related amyloidoses. Mechanism-based strategies for inhibiting protein aggregation and potential therapeutic applications in different diseases.

Amyloid. --- Degeneration (Pathology). --- Amyloidosis --- Amyloid --- Nervous System Diseases --- Noxae --- Proteins --- Toxic Actions --- Diseases --- Chemical Actions and Uses --- Amino Acids, Peptides, and Proteins --- Chemicals and Drugs --- Cytotoxins --- Neurodegenerative Diseases --- Amyloidogenic Proteins --- Human Anatomy & Physiology --- Health & Biological Sciences --- Animal Biochemistry --- Amyloidosis. --- Protein binding. --- Degeneration (Pathology) --- Degenerative diseases --- Degenerative disorders --- Binding, Protein --- Amyloid degeneration --- Medicine. --- Neurosciences. --- Pathology. --- Proteins. --- Neurobiology. --- Biomedicine. --- Biomedicine general. --- Protein Science. --- Protein Structure. --- Pathology --- Biochemistry --- Allosteric proteins --- Radioligand assay --- Lymphoproliferative disorders --- Metabolism --- Disorders --- Biochemistry. --- Disease (Pathology) --- Medical sciences --- Medicine --- Medicine, Preventive --- Neurosciences --- Neural sciences --- Neurological sciences --- Neuroscience --- Nervous system --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Chemistry --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Physicians --- Composition --- Proteins . --- Biomedicine, general. --- Health Workforce --- Proteids --- Biomolecules --- Polypeptides --- Proteomics