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Spider silk protein...
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Qi, XingmeiThe Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China
(författare)
Spider silk protein forms amyloid-like nanofibrils through a non-nucleation-dependent polymerization mechanism
- Artikel/kapitelEngelska2023
Förlag, utgivningsår, omfång ...
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John Wiley & Sons,2023
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electronicrdacarrier
Nummerbeteckningar
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LIBRIS-ID:oai:DiVA.org:umu-212398
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https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-212398URI
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https://doi.org/10.1002/smll.202304031DOI
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http://kipublications.ki.se/Default.aspx?queryparsed=id:153318103URI
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Språk:engelska
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Sammanfattning på:engelska
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Ämneskategori:ref swepub-contenttype
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Ämneskategori:art swepub-publicationtype
Anmärkningar
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Amyloid fibrils—nanoscale fibrillar aggregates with high levels of order—are pathogenic in some today incurable human diseases; however, there are also many physiologically functioning amyloids in nature. The process of amyloid formation is typically nucleation-elongation-dependent, as exemplified by the pathogenic amyloid-β peptide (Aβ) that is associated with Alzheimer's disease. Spider silk, one of the toughest biomaterials, shares characteristics with amyloid. In this study, it is shown that forming amyloid-like nanofibrils is an inherent property preserved by various spider silk proteins (spidroins). Both spidroins and Aβ capped by spidroin N- and C-terminal domains, can assemble into macroscopic spider silk-like fibers that consist of straight nanofibrils parallel to the fiber axis as observed in native spider silk. While Aβ forms amyloid nanofibrils through a nucleation-dependent pathway and exhibits strong cytotoxicity and seeding effects, spidroins spontaneously and rapidly form amyloid-like nanofibrils via a non-nucleation-dependent polymerization pathway that involves lateral packing of fibrils. Spidroin nanofibrils share amyloid-like properties but lack strong cytotoxicity and the ability to self-seed or cross-seed human amyloidogenic peptides. These results suggest that spidroins' unique primary structures have evolved to allow functional properties of amyloid, and at the same time direct their fibrillization pathways to avoid formation of cytotoxic intermediates.
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Wang, YuDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden; College of Wildlife and Protected Area, Northeast Forestry University, Harbin, China
(författare)
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Yu, HairuiThe Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China
(författare)
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Liu, RuifangThe Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China
(författare)
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Leppert, AxelDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Solna, Sweden
(författare)
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Zheng, ZihanDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden; Department of Pharmacology, Xi'an Jiaotong University, Shaanxi, China
(författare)
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Zhong, XueyingSchool of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Biomedical Engineering and Health Systems, KTH Royal Institute of Technology, Huddinge, Sweden
(författare)
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Jin, ZhenDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden; Department of Pharmacology, Xi'an Jiaotong University, Shaanxi, China
(författare)
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Wang, HanThe Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China
(författare)
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Li, XiaoliDepartment of Pharmacology, College of Pharmacy, Chongqing Medical University, Chongqing, China
(författare)
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Wang, XiuzheDepartment of Neurology, Shanghai Sixth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China
(författare)
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Landreh, MichaelDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Solna, Sweden
(författare)
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Morozova-Roche, Ludmilla A.Umeå universitet,Institutionen för medicinsk kemi och biofysik(Swepub:umu)lumo0001
(författare)
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Johansson, JanKarolinska Institutet
(författare)
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Xiong, SidongThe Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China
(författare)
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Iashchishyn, IgorUmeå universitet,Institutionen för medicinsk kemi och biofysik(Swepub:umu)igia0001
(författare)
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Chen, GefeiDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden
(författare)
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The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, ChinaDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden; College of Wildlife and Protected Area, Northeast Forestry University, Harbin, China
(creator_code:org_t)
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Ingår i:Small: John Wiley & Sons18:461613-68101613-6829
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Qi, Xingmei
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Wang, Yu
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Yu, Hairui
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Liu, Ruifang
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Leppert, Axel
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Zheng, Zihan
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visa fler...
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Zhong, Xueying
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Jin, Zhen
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Wang, Han
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Li, Xiaoli
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Wang, Xiuzhe
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Landreh, Michael
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Morozova-Roche, ...
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Johansson, Jan
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Xiong, Sidong
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Iashchishyn, Igo ...
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Chen, Gefei
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