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: | Online |
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| Language: | English |
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MDPI - Multidisciplinary Digital Publishing Institute
2022
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| Online Access: | ONIX_20220506_9783036526911_267 |
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| collection | Directory of Open Access Books |
| description | 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. |
| format | Online |
| id | doab-20.500.12854ir-81201 |
| institution | Directory of Open Access Books |
| language | eng |
| publishDate | 2022 |
| publishDateRange | 2022 |
| publishDateSort | 2022 |
| publisher | MDPI - Multidisciplinary Digital Publishing Institute |
| publisherStr | MDPI - Multidisciplinary Digital Publishing Institute |
| record_format | ojs |
| spelling | doab-20.500.12854ir-812012024-03-28T03:31:10Z Protein Adsorption and Conformational Changes Assfalg, Michael 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 n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PSB Biochemistry 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. 2022-05-06T11:35:02Z 2022-05-06T11:35:02Z 2022 book ONIX_20220506_9783036526911_267 9783036526911 9783036526904 https://directory.doabooks.org/handle/20.500.12854/81201 eng image/jpeg Attribution 4.0 International https://mdpi.com/books/pdfview/book/5233 https://mdpi.com/books/pdfview/book/5233 MDPI - Multidisciplinary Digital Publishing Institute 10.3390/books978-3-0365-2690-4 10.3390/books978-3-0365-2690-4 46cabcaa-dd94-4bfe-87b4-55023c1b36d0 9783036526911 9783036526904 100 Basel open access |
| spellingShingle | 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 n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PSB Biochemistry Protein Adsorption and Conformational Changes |
| title | Protein Adsorption and Conformational Changes |
| title_full | Protein Adsorption and Conformational Changes |
| title_fullStr | Protein Adsorption and Conformational Changes |
| title_full_unstemmed | Protein Adsorption and Conformational Changes |
| title_short | Protein Adsorption and Conformational Changes |
| title_sort | protein adsorption and conformational changes |
| topic | 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 n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PSB Biochemistry |
| topic_facet | 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 n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences thema EDItEUR::P Mathematics and Science::PS Biology, life sciences::PSB Biochemistry |
| url | ONIX_20220506_9783036526911_267 |