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蜘蛛丝蛋白核心结构域离子和种子依赖性原纤维组装的数据。

Data for ion and seed dependent fibril assembly of a spidroin core domain.

作者信息

Humenik Martin, Smith Andrew M, Arndt Sina, Scheibel Thomas

机构信息

Biomaterials, Faculty of Engineering Science, Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, Germany.

Biomaterials, Faculty of Engineering Science, Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, Germany ; Bayreuth Center for Colloids and Interfaces (BZKG), Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, Germany ; Research Center Bio-Macromolecules (BIOmac), Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, Germany ; Bayreuth Center for Molecular Biosciences (BZMB), Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, Germany ; Bayreuth Center for Material Science (BayMAT), Universität Bayreuth, Universitätsstraße 30, 95440 Bayreuth, Germany.

出版信息

Data Brief. 2015 Jul 29;4:571-6. doi: 10.1016/j.dib.2015.07.023. eCollection 2015 Sep.

DOI:10.1016/j.dib.2015.07.023
PMID:26322321
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4543078/
Abstract

This data article includes size exclusion chromatography data of soluble eADF4(C16), an engineered spider silk variant based on the core domain sequence of the natural dragline silk protein ADF4 of Araneus diadematus, in combination with light scattering; the protein is monomeric before assembly. The assembled mature fibrils were visualized by transmission electron microscopy (TEM) and atomic force microscopy (AFM). Sonicated fibrils were used as seeds to by-pass the nucleation lag phase in eADF4(C16) assembly. We also provide data on the sedimentation kinetics of spider silk in the presence of different NaCl concentrations revealing very slow protein aggregation in comparison to the fast assembly triggered by phosphate ions published previously [1]. Experiments in the Data article represent supporting material for our work published recently [1], which described the assembly mechanism of recombinant eADF4(C16) fibrils.

摘要

本数据文章包含可溶性eADF4(C16)的尺寸排阻色谱数据,eADF4(C16)是一种基于十字园蛛天然拖牵丝蛋白ADF4核心结构域序列构建的蜘蛛丝变体,并结合了光散射;该蛋白在组装前为单体。通过透射电子显微镜(TEM)和原子力显微镜(AFM)观察组装后的成熟纤维。超声处理的纤维用作种子,以绕过eADF4(C16)组装中的成核延迟阶段。我们还提供了在不同NaCl浓度下蜘蛛丝沉降动力学的数据,揭示了与先前发表的由磷酸根离子触发的快速组装相比非常缓慢的蛋白质聚集[1]。本数据文章中的实验为我们最近发表的工作[1]提供了支持材料,该工作描述了重组eADF4(C16)纤维的组装机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c22a/4543078/b1d5fc5b3818/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c22a/4543078/a58a0be5b1ff/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c22a/4543078/ab17d1124931/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c22a/4543078/f5e8485cb9ef/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c22a/4543078/747543998387/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c22a/4543078/5526becd5116/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c22a/4543078/b1d5fc5b3818/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c22a/4543078/a58a0be5b1ff/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c22a/4543078/ab17d1124931/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c22a/4543078/f5e8485cb9ef/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c22a/4543078/747543998387/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c22a/4543078/5526becd5116/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c22a/4543078/b1d5fc5b3818/gr6.jpg

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本文引用的文献

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J Struct Biol. 2015 Aug;191(2):130-8. doi: 10.1016/j.jsb.2015.06.021. Epub 2015 Jun 27.
2
Biomimetic fibers made of recombinant spidroins with the same toughness as natural spider silk.具有与天然蜘蛛丝一样韧性的重组蜘蛛丝仿生纤维。
Adv Mater. 2015 Apr 1;27(13):2189-94. doi: 10.1002/adma.201404234. Epub 2015 Feb 16.
3
Influence of repeat numbers on self-assembly rates of repetitive recombinant spider silk proteins.
末端球状结构域对重组 mini 蛛丝蛋白响应纤维纺丝触发物的影响。
Sci Rep. 2020 Jun 30;10(1):10671. doi: 10.1038/s41598-020-67703-1.
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Synthetic biology for fibres, adhesives and active camouflage materials in protection and aerospace.用于防护和航空航天领域的纤维、粘合剂及主动伪装材料的合成生物学。
MRS Commun. 2019 May 15;9(2):486-504. doi: 10.1557/mrc.2019.35. Epub 2019 Apr 24.
重复序列数量对重复重组蜘蛛丝蛋白自组装速率的影响。
J Struct Biol. 2014 Jun;186(3):431-7. doi: 10.1016/j.jsb.2014.03.010. Epub 2014 Mar 20.
4
Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation.揭示亨廷顿蛋白外显子 1 的 N 端和 C 端侧翼序列作为多聚谷氨酰胺聚集调节剂的作用。
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Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism.β淀粉样蛋白 42 聚集物的增殖通过二级成核机制发生。
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Fitting neurological protein aggregation kinetic data via a 2-step, minimal/"Ockham's razor" model: the Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth.通过两步、最小化/“奥卡姆剃刀”模型拟合神经学蛋白质聚集动力学数据:成核的芬克-瓦茨基机制,随后是自催化表面生长。
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Spider silk and amyloid fibrils: a structural comparison.蜘蛛丝与淀粉样纤维:结构比较
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