Gold nanoparticles as amyloid-like fibrillogenesis inhibitors
•Nanoparticles can cross blood-brain-barrier and target amyloidogenic structures.•AuNPs affect the protein structure and dynamics of insulin fibril for aggregation.•AuNPs delayed amyloid-like fibrils formation by about 1 week.•AuNPs disrupt fibrillogenesis resulting in fibrils are shorter and more c...
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| Veröffentlicht in: | Colloids and surfaces, B, Biointerfaces B, Biointerfaces, 2013-12, Vol.112, p.525-529 |
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| creator | Hsieh, Shuchen Chang, Chiung-wen Chou, Hsuan-hung |
| description | •Nanoparticles can cross blood-brain-barrier and target amyloidogenic structures.•AuNPs affect the protein structure and dynamics of insulin fibril for aggregation.•AuNPs delayed amyloid-like fibrils formation by about 1 week.•AuNPs disrupt fibrillogenesis resulting in fibrils are shorter and more compact.
Amyloid aggregates are one of the likely key factors leading to the development of Alzheimer's disease (AD) and other amyloidosis associated diseases. Several recent studies have shown that some anti-diabetic drugs have a positive therapeutic effect on AD patients by crossing the blood brain barrier (BBB) and preventing or reducing insulin resistance. Nanoparticles (NPs) or nanoscale objects ( |
| doi_str_mv | 10.1016/j.colsurfb.2013.08.029 |
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Amyloid aggregates are one of the likely key factors leading to the development of Alzheimer's disease (AD) and other amyloidosis associated diseases. Several recent studies have shown that some anti-diabetic drugs have a positive therapeutic effect on AD patients by crossing the blood brain barrier (BBB) and preventing or reducing insulin resistance. Nanoparticles (NPs) or nanoscale objects (<600Da.), are able to cross the BBB at low concentrations, and can specifically target amyloidogenic structures. Thus, NPs are fast becoming indispensable tools for directed drug delivery, particularly when targeting structures or regions in the brain. Here, we have explored the inhibitory effect of gold nanoparticles (AuNPs) on the fibrillogenesis process of insulin fibrils. We found that when AuNPs were co-incubated with insulin, the structural transformation into amyloid-like fibrils was delayed by about a week. Further, the fibrils that formed, exhibited altered structure, shape, and dynamics, which further reduced fibril growth, and the stability of available amyloid-like fibrils with cross-β structure for aggregation. Our results demonstrate that AuNPs disrupt insulin amyloid fibrillation resulting in fibrils that are shorter and more compact, and thus may serve a useful role in new therapeutic and diagnostic strategies for amyloid-related disorders.</description><identifier>ISSN: 0927-7765</identifier><identifier>EISSN: 1873-4367</identifier><identifier>DOI: 10.1016/j.colsurfb.2013.08.029</identifier><identifier>PMID: 24060166</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>AFM ; Alzheimer disease ; Alzheimer Disease - drug therapy ; Alzheimer Disease - metabolism ; Alzheimer's ; amyloid ; Amyloid - antagonists & inhibitors ; Amyloid - chemistry ; Amyloid - ultrastructure ; Amyloid fibril ; amyloidosis ; Animals ; Blood-Brain Barrier ; Brain ; Cattle ; Circular Dichroism ; colloids ; Diseases ; Drug Delivery Systems ; Gold ; Gold - chemistry ; Humans ; hypoglycemic agents ; Inhibitors ; Insulin ; Insulin - chemistry ; insulin resistance ; Metal Nanoparticles - chemistry ; Microscopy, Atomic Force ; Microscopy, Electron, Transmission ; nanogold ; Nanoparticle ; Nanoparticles ; Nanostructure ; patients ; Protein Multimerization - drug effects ; therapeutics</subject><ispartof>Colloids and surfaces, B, Biointerfaces, 2013-12, Vol.112, p.525-529</ispartof><rights>2013 Elsevier B.V.</rights><rights>Copyright © 2013 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c458t-3bc7a7004f21f016bee8badf37679317fd70463de9705106e9bbc2099987269e3</citedby><cites>FETCH-LOGICAL-c458t-3bc7a7004f21f016bee8badf37679317fd70463de9705106e9bbc2099987269e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.colsurfb.2013.08.029$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24060166$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hsieh, Shuchen</creatorcontrib><creatorcontrib>Chang, Chiung-wen</creatorcontrib><creatorcontrib>Chou, Hsuan-hung</creatorcontrib><title>Gold nanoparticles as amyloid-like fibrillogenesis inhibitors</title><title>Colloids and surfaces, B, Biointerfaces</title><addtitle>Colloids Surf B Biointerfaces</addtitle><description>•Nanoparticles can cross blood-brain-barrier and target amyloidogenic structures.•AuNPs affect the protein structure and dynamics of insulin fibril for aggregation.•AuNPs delayed amyloid-like fibrils formation by about 1 week.•AuNPs disrupt fibrillogenesis resulting in fibrils are shorter and more compact.
Amyloid aggregates are one of the likely key factors leading to the development of Alzheimer's disease (AD) and other amyloidosis associated diseases. Several recent studies have shown that some anti-diabetic drugs have a positive therapeutic effect on AD patients by crossing the blood brain barrier (BBB) and preventing or reducing insulin resistance. Nanoparticles (NPs) or nanoscale objects (<600Da.), are able to cross the BBB at low concentrations, and can specifically target amyloidogenic structures. Thus, NPs are fast becoming indispensable tools for directed drug delivery, particularly when targeting structures or regions in the brain. Here, we have explored the inhibitory effect of gold nanoparticles (AuNPs) on the fibrillogenesis process of insulin fibrils. We found that when AuNPs were co-incubated with insulin, the structural transformation into amyloid-like fibrils was delayed by about a week. Further, the fibrils that formed, exhibited altered structure, shape, and dynamics, which further reduced fibril growth, and the stability of available amyloid-like fibrils with cross-β structure for aggregation. Our results demonstrate that AuNPs disrupt insulin amyloid fibrillation resulting in fibrils that are shorter and more compact, and thus may serve a useful role in new therapeutic and diagnostic strategies for amyloid-related disorders.</description><subject>AFM</subject><subject>Alzheimer disease</subject><subject>Alzheimer Disease - drug therapy</subject><subject>Alzheimer Disease - metabolism</subject><subject>Alzheimer's</subject><subject>amyloid</subject><subject>Amyloid - antagonists & inhibitors</subject><subject>Amyloid - chemistry</subject><subject>Amyloid - ultrastructure</subject><subject>Amyloid fibril</subject><subject>amyloidosis</subject><subject>Animals</subject><subject>Blood-Brain Barrier</subject><subject>Brain</subject><subject>Cattle</subject><subject>Circular Dichroism</subject><subject>colloids</subject><subject>Diseases</subject><subject>Drug Delivery Systems</subject><subject>Gold</subject><subject>Gold - chemistry</subject><subject>Humans</subject><subject>hypoglycemic agents</subject><subject>Inhibitors</subject><subject>Insulin</subject><subject>Insulin - chemistry</subject><subject>insulin resistance</subject><subject>Metal Nanoparticles - chemistry</subject><subject>Microscopy, Atomic Force</subject><subject>Microscopy, Electron, Transmission</subject><subject>nanogold</subject><subject>Nanoparticle</subject><subject>Nanoparticles</subject><subject>Nanostructure</subject><subject>patients</subject><subject>Protein Multimerization - drug effects</subject><subject>therapeutics</subject><issn>0927-7765</issn><issn>1873-4367</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1vEzEQhq2KiobCXyg5ctll_LH2-oAEqqAgVeJQerZs77h1cNbB3lTqv8dRWq5FGsmXZ94Zz0PIBYWeApUfN73Pqe5LcD0DynsYe2D6hKzoqHgnuFSvyAo0U51Scjgjb2rdAAATVL0mZ0yAbClyRT5d5TStZzvnnS1L9Anr2rbaPqYcpy7F37gO0ZWYUr7DGWus6zjfRxeXXOpbchpsqvju6T0nt9--_rr83l3_vPpx-eW682IYl447r6wCEIHR0OY6xNHZKXAlleZUhUmBkHxCrWCgIFE75xlorUfFpEZ-Tj4cc3cl_9ljXcw2Vo8p2RnzvhoqByoGqiT8ByqYpIzD8DIqhGYjYwNtqDyivuRaCwazK3Fry6OhYA5CzMY8CzEHIQZG04S0xounGXu3xelf27OBBrw_AsFmY-9KrOb2piXIZou3cxx-9PlIYLvwQ8Riqo84e5xiQb-YKceXtvgL01mnbA</recordid><startdate>20131201</startdate><enddate>20131201</enddate><creator>Hsieh, Shuchen</creator><creator>Chang, Chiung-wen</creator><creator>Chou, Hsuan-hung</creator><general>Elsevier B.V</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>JG9</scope><scope>L7M</scope></search><sort><creationdate>20131201</creationdate><title>Gold nanoparticles as amyloid-like fibrillogenesis inhibitors</title><author>Hsieh, Shuchen ; Chang, Chiung-wen ; Chou, Hsuan-hung</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c458t-3bc7a7004f21f016bee8badf37679317fd70463de9705106e9bbc2099987269e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>AFM</topic><topic>Alzheimer disease</topic><topic>Alzheimer Disease - drug therapy</topic><topic>Alzheimer Disease - metabolism</topic><topic>Alzheimer's</topic><topic>amyloid</topic><topic>Amyloid - antagonists & inhibitors</topic><topic>Amyloid - chemistry</topic><topic>Amyloid - ultrastructure</topic><topic>Amyloid fibril</topic><topic>amyloidosis</topic><topic>Animals</topic><topic>Blood-Brain Barrier</topic><topic>Brain</topic><topic>Cattle</topic><topic>Circular Dichroism</topic><topic>colloids</topic><topic>Diseases</topic><topic>Drug Delivery Systems</topic><topic>Gold</topic><topic>Gold - chemistry</topic><topic>Humans</topic><topic>hypoglycemic agents</topic><topic>Inhibitors</topic><topic>Insulin</topic><topic>Insulin - chemistry</topic><topic>insulin resistance</topic><topic>Metal Nanoparticles - chemistry</topic><topic>Microscopy, Atomic Force</topic><topic>Microscopy, Electron, Transmission</topic><topic>nanogold</topic><topic>Nanoparticle</topic><topic>Nanoparticles</topic><topic>Nanostructure</topic><topic>patients</topic><topic>Protein Multimerization - drug effects</topic><topic>therapeutics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hsieh, Shuchen</creatorcontrib><creatorcontrib>Chang, Chiung-wen</creatorcontrib><creatorcontrib>Chou, Hsuan-hung</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><jtitle>Colloids and surfaces, B, Biointerfaces</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hsieh, Shuchen</au><au>Chang, Chiung-wen</au><au>Chou, Hsuan-hung</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Gold nanoparticles as amyloid-like fibrillogenesis inhibitors</atitle><jtitle>Colloids and surfaces, B, Biointerfaces</jtitle><addtitle>Colloids Surf B Biointerfaces</addtitle><date>2013-12-01</date><risdate>2013</risdate><volume>112</volume><spage>525</spage><epage>529</epage><pages>525-529</pages><issn>0927-7765</issn><eissn>1873-4367</eissn><abstract>•Nanoparticles can cross blood-brain-barrier and target amyloidogenic structures.•AuNPs affect the protein structure and dynamics of insulin fibril for aggregation.•AuNPs delayed amyloid-like fibrils formation by about 1 week.•AuNPs disrupt fibrillogenesis resulting in fibrils are shorter and more compact.
Amyloid aggregates are one of the likely key factors leading to the development of Alzheimer's disease (AD) and other amyloidosis associated diseases. Several recent studies have shown that some anti-diabetic drugs have a positive therapeutic effect on AD patients by crossing the blood brain barrier (BBB) and preventing or reducing insulin resistance. Nanoparticles (NPs) or nanoscale objects (<600Da.), are able to cross the BBB at low concentrations, and can specifically target amyloidogenic structures. Thus, NPs are fast becoming indispensable tools for directed drug delivery, particularly when targeting structures or regions in the brain. Here, we have explored the inhibitory effect of gold nanoparticles (AuNPs) on the fibrillogenesis process of insulin fibrils. We found that when AuNPs were co-incubated with insulin, the structural transformation into amyloid-like fibrils was delayed by about a week. Further, the fibrils that formed, exhibited altered structure, shape, and dynamics, which further reduced fibril growth, and the stability of available amyloid-like fibrils with cross-β structure for aggregation. Our results demonstrate that AuNPs disrupt insulin amyloid fibrillation resulting in fibrils that are shorter and more compact, and thus may serve a useful role in new therapeutic and diagnostic strategies for amyloid-related disorders.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>24060166</pmid><doi>10.1016/j.colsurfb.2013.08.029</doi><tpages>5</tpages></addata></record> |
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| subjects | AFM Alzheimer disease Alzheimer Disease - drug therapy Alzheimer Disease - metabolism Alzheimer's amyloid Amyloid - antagonists & inhibitors Amyloid - chemistry Amyloid - ultrastructure Amyloid fibril amyloidosis Animals Blood-Brain Barrier Brain Cattle Circular Dichroism colloids Diseases Drug Delivery Systems Gold Gold - chemistry Humans hypoglycemic agents Inhibitors Insulin Insulin - chemistry insulin resistance Metal Nanoparticles - chemistry Microscopy, Atomic Force Microscopy, Electron, Transmission nanogold Nanoparticle Nanoparticles Nanostructure patients Protein Multimerization - drug effects therapeutics |
| title | Gold nanoparticles as amyloid-like fibrillogenesis inhibitors |
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