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Spider silk protein forms amyloid-like nanofibrils through a non-nucleation-dependent polymerization mechanism

Qi, Xingmei (författare)
The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China,Soochow Univ, Jiangsu Key Lab Infect & Immun, Inst Biol & Med Sci, Suzhou 215123, Peoples R China.
Wang, Yu (författare)
Department of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden; College of Wildlife and Protected Area, Northeast Forestry University, Harbin, China,Karolinska Inst, Dept Biosci & Nutr, S-14157 Huddinge, Sweden.;Northeast Forestry Univ, Coll Wildlife & Protected Area, Harbin 150040, Peoples R China.
Yu, Hairui (författare)
The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China,Soochow Univ, Jiangsu Key Lab Infect & Immun, Inst Biol & Med Sci, Suzhou 215123, Peoples R China.
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Liu, Ruifang (författare)
The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China,Soochow Univ, Jiangsu Key Lab Infect & Immun, Inst Biol & Med Sci, Suzhou 215123, Peoples R China.
Leppert, Axel (författare)
Karolinska Institutet
Zheng, Zihan (författare)
Department of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden; Department of Pharmacology, Xi'an Jiaotong University, Shaanxi, China,Karolinska Inst, Dept Biosci & Nutr, S-14157 Huddinge, Sweden.;Xi An Jiao Tong Univ, Dept Pharmacol, Xian 710061, Shaanxi, Peoples R China.
Zhong, Xueying (författare)
KTH,Strukturell bioteknik
Jin, Zhen (författare)
Department of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden; Department of Pharmacology, Xi'an Jiaotong University, Shaanxi, China,Karolinska Inst, Dept Biosci & Nutr, S-14157 Huddinge, Sweden.;Xi An Jiao Tong Univ, Dept Pharmacol, Xian 710061, Shaanxi, Peoples R China.
Wang, Han (författare)
The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China,Soochow Univ, Jiangsu Key Lab Infect & Immun, Inst Biol & Med Sci, Suzhou 215123, Peoples R China.
Li, Xiaoli (författare)
Department of Pharmacology, College of Pharmacy, Chongqing Medical University, Chongqing, China,Chongqing Med Univ, Dept Pharmacol, Coll Pharm, Chongqing 400016, Peoples R China.
Wang, Xiuzhe (författare)
Department of Neurology, Shanghai Sixth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China,Shanghai Jiao Tong Univ, Dept Neurol, Sch Med, Shanghai Peoples Hosp 6, Shanghai 200233, Peoples R China.
Landreh, Michael (författare)
Karolinska Institutet
Morozova-Roche, Ludmilla A. (författare)
Umeå universitet,Institutionen för medicinsk kemi och biofysik,Umeå Univ, Dept Med Biochem & Biophys, S-90187 Umeå, Sweden.
Johansson, Jan (författare)
Karolinska Institutet
Xiong, Sidong (författare)
The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China,Soochow Univ, Jiangsu Key Lab Infect & Immun, Inst Biol & Med Sci, Suzhou 215123, Peoples R China.
Iashchishyn, Igor (författare)
Umeå universitet,Institutionen för medicinsk kemi och biofysik,Umeå Univ, Dept Med Biochem & Biophys, S-90187 Umeå, Sweden.
Chen, Gefei (författare)
Karolinska Institutet
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The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China Soochow Univ, Jiangsu Key Lab Infect & Immun, Inst Biol & Med Sci, Suzhou 215123, Peoples R China (creator_code:org_t)
John Wiley & Sons, 2023
2023
Engelska.
Ingår i: Small. - : John Wiley & Sons. - 1613-6810 .- 1613-6829. ; 18:46
Relaterad länk:
https://doi.org/10.1...
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https://umu.diva-por... (primary) (Raw object)
https://urn.kb.se/re...
https://doi.org/10.1...
https://urn.kb.se/re...
http://kipublication...
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  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • 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.

Ämnesord

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
NATURVETENSKAP  -- Biologi -- Strukturbiologi (hsv//swe)
NATURAL SCIENCES  -- Biological Sciences -- Structural Biology (hsv//eng)

Nyckelord

cytotoxicity
nanofibril
non-nucleation-dependent polymerization
seeding
spidroin

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