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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
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003SwePub
008240213s2023 | |||||||||||000 ||eng|
009oai:DiVA.org:umu-212398
009oai:prod.swepub.kib.ki.se:153318103
024a https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-3434032 URI
024a https://doi.org/10.1002/smll.2023040312 DOI
024a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-2123982 URI
024a http://kipublications.ki.se/Default.aspx?queryparsed=id:1533181032 URI
040 a (SwePub)kthd (SwePub)umud (SwePub)ki
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
100a Qi, Xingmeiu Soochow Univ, Jiangsu Key Lab Infect & Immun, Inst Biol & Med Sci, Suzhou 215123, Peoples R China.,The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China4 aut
2451 0a Spider Silk Protein Forms Amyloid-Like Nanofibrils through a Non-Nucleation-Dependent Polymerization Mechanism (Small 46/2023)
264 1b Wiley,c 2023
338 a print2 rdacarrier
500 a QC 20240213
520 a 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.
650 7a NATURVETENSKAPx Biologix Strukturbiologi0 (SwePub)106012 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Structural Biology0 (SwePub)106012 hsv//eng
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
653 a cytotoxicity
653 a nanofibril
653 a non-nucleation-dependent polymerization
653 a seeding
653 a spidroin
700a Wang, Yuu Karolinska Inst, Dept Biosci & Nutr, S-14157 Huddinge, Sweden.;Northeast Forestry Univ, Coll Wildlife & Protected Area, Harbin 150040, Peoples R China.,Department of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden; College of Wildlife and Protected Area, Northeast Forestry University, Harbin, China4 aut
700a Yu, Hairuiu Soochow Univ, Jiangsu Key Lab Infect & Immun, Inst Biol & Med Sci, Suzhou 215123, Peoples R China.,The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China4 aut
700a Liu, Ruifangu Soochow Univ, Jiangsu Key Lab Infect & Immun, Inst Biol & Med Sci, Suzhou 215123, Peoples R China.,The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China4 aut
700a Leppert, Axelu Karolinska Institutet4 aut
700a Zheng, Zihanu Karolinska Inst, Dept Biosci & Nutr, S-14157 Huddinge, Sweden.;Xi An Jiao Tong Univ, Dept Pharmacol, Xian 710061, Shaanxi, Peoples R China.,Department of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden; Department of Pharmacology, Xi'an Jiaotong University, Shaanxi, China4 aut
700a Zhong, Xueyingu KTH,Strukturell bioteknik,School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Biomedical Engineering and Health Systems, KTH Royal Institute of Technology, Huddinge, Sweden4 aut0 (Swepub:kth)u169038p
700a Jin, Zhenu Karolinska Inst, Dept Biosci & Nutr, S-14157 Huddinge, Sweden.;Xi An Jiao Tong Univ, Dept Pharmacol, Xian 710061, Shaanxi, Peoples R China.,Department of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden; Department of Pharmacology, Xi'an Jiaotong University, Shaanxi, China4 aut
700a Wang, Hanu Soochow Univ, Jiangsu Key Lab Infect & Immun, Inst Biol & Med Sci, Suzhou 215123, Peoples R China.,The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China4 aut
700a Li, Xiaoliu Chongqing Med Univ, Dept Pharmacol, Coll Pharm, Chongqing 400016, Peoples R China.,Department of Pharmacology, College of Pharmacy, Chongqing Medical University, Chongqing, China4 aut
700a Wang, Xiuzheu Shanghai Jiao Tong Univ, Dept Neurol, Sch Med, Shanghai Peoples Hosp 6, Shanghai 200233, Peoples R China.,Department of Neurology, Shanghai Sixth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China4 aut
700a Landreh, Michaelu Karolinska Institutet4 aut
700a Morozova-Roche, Ludmilla A.u Umeå universitet,Institutionen för medicinsk kemi och biofysik,Umeå Univ, Dept Med Biochem & Biophys, S-90187 Umeå, Sweden.4 aut0 (Swepub:umu)lumo0001
700a Johansson, Janu Karolinska Institutet4 aut
700a Xiong, Sidongu Soochow Univ, Jiangsu Key Lab Infect & Immun, Inst Biol & Med Sci, Suzhou 215123, Peoples R China.,The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China4 aut
700a Iashchishyn, Igoru Umeå universitet,Institutionen för medicinsk kemi och biofysik,Umeå Univ, Dept Med Biochem & Biophys, S-90187 Umeå, Sweden.4 aut0 (Swepub:umu)igia0001
700a Chen, Gefeiu Karolinska Institutet4 aut
710a Soochow Univ, Jiangsu Key Lab Infect & Immun, Inst Biol & Med Sci, Suzhou 215123, Peoples R China.b The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China4 org
773t Smalld : Wileyg 19:46q 19:46x 1613-6810x 1613-6829
856u https://doi.org/10.1002/smll.202304031y Fulltext
856u https://umu.diva-portal.org/smash/get/diva2:1784762/FULLTEXT02.pdfx primaryx Raw objecty fulltext:print
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-343403
8564 8u https://doi.org/10.1002/smll.202304031
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-212398
8564 8u http://kipublications.ki.se/Default.aspx?queryparsed=id:153318103

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