| 1. |
- Qi, Xingmei, et al.
(författare)
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Spider silk protein forms amyloid-like nanofibrils through a non-nucleation-dependent polymerization mechanism
- 2023
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Ingår i: Small. - : John Wiley & Sons. - 1613-6810 .- 1613-6829. ; 18:46
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Tidskriftsartikel (refereegranskat)abstract
- 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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| 2. |
- Qi, Xingmei, et al.
(författare)
-
Spider Silk Protein Forms Amyloid-Like Nanofibrils through a Non-Nucleation-Dependent Polymerization Mechanism (Small 46/2023)
- 2023
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Ingår i: Small. - : Wiley. - 1613-6810 .- 1613-6829. ; 19:46
-
Tidskriftsartikel (refereegranskat)abstract
- 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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| 3. |
- Qi, Xingmei, et al.
(författare)
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Spiders use structural conversion of globular amyloidogenic domains to make strong silk fibers
- 2024
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Ingår i: Advanced Functional Materials. - : Wiley-VCH Verlagsgesellschaft. - 1616-301X .- 1616-3028. ; 34:23
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Tidskriftsartikel (refereegranskat)abstract
- Spider silk—an environmentally friendly protein-based material—is widely recognized for its extraordinary mechanical properties. Biomimetic spider silk-like fibers made from recombinant spider silk proteins (spidroins) currently falls short compared to natural silks in terms of mechanical performance. In this study, it is discovered that spiders use structural conversion of molecular enhancers—conserved globular 127-residue spacer domains—to make strong silk fibers. This domain lacks poly-Ala motifs but interestingly contains motifs that are similar to human amyloidogenic motifs, and that it self-assembles into amyloid-like fibrils through a non-nucleation-dependent pathway, likely to avoid the formation of cytotoxic intermediates. Incorporating this spacer domain into a recombinant chimeric spidroin facilitates self-assembly into silk-like fibers, increases fiber molecular homogeneity, and markedly enhances fiber mechanical strength. These findings highlight that spiders employ diverse strategies to produce silk with exceptional mechanical properties. The spacer domain offers a way to enhance the properties of recombinant spider silk-like fibers and other functional materials.
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| 4. |
- Yang, Xingmei, et al.
(författare)
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Protection efficiency of side airbag on child occupant
- 2011
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Ingår i: Jiangsu Daxue Xuebao (Ziran Kexue Ban) / Journal of Jiangsu University (Natural Science Edition). - 1671-7775. ; 32:4, s. 379-384, id. 1671-7775(2011)04-0000-0-
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Tidskriftsartikel (refereegranskat)abstract
- The aim of this paper is to evaluate the injury risk of child occupant exposed to the deployed side airbag in side impact. Based on the Prescribed Structure Motion, LS-Dyna and MADYMO softwares was used to develop the simulation models. Simulations with and without side airbag deployment were carried out under the Euro-NCAP side impact conditions. The dynamic response parameters of head, neck and thorax of 6-year-old child with misusing and using correctly booster seat were analyzed and compared. The results indicated that the child misusing booster seat may not receive the threat of side airbag for head and thorax. The child using booster seat correctly may receive the protective benefits of side airbag for head and thorax. Whether a child misuses or uses correctly booster seat, the injury risk of neck depends on the real impact situations.
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