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末端酪氨酸 10 的卤化促进了淀粉样-β序列 7-12 的超分子稳定化。

Halogenation of the -Terminus Tyrosine 10 Promotes Supramolecular Stabilization of the Amyloid-β Sequence 7-12.

机构信息

Dept. Chem., Mater., and Chem. Eng. "Giulio Natta" Politecnico di Milano Via L. Mancinelli 7 20131 Milano Italy.

Istituto di Scienze e Tecnologie Chimiche National Research Council of Italy Via M. Bianco 9 20131 Milano Italy.

出版信息

ChemistryOpen. 2020 Feb 25;9(2):253-260. doi: 10.1002/open.201900350. eCollection 2020 Feb.

DOI:10.1002/open.201900350
PMID:32110506
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7041548/
Abstract

Here, we demonstrate that introduction of halogen atoms at the tyrosine 10 phenol ring of the DSGYEV sequence derived from the flexible amyloid-β -terminus, promotes its self-assembly in the solid state. In particular, we report the crystal structures of two halogen-modified sequences, which we found to be stabilized in the solid state by halogen-mediated interactions. The structural study is corroborated by Non-Covalent Interaction (NCI) analysis. Our results prove that selective halogenation of an amino acid enhances the supramolecular organization of otherwise unstructured biologically-relevant sequences. This method may develop as a general strategy for stabilizing highly polymorphic peptide regions.

摘要

在这里，我们证明了在源自柔性淀粉样β-末端的 DSGYEV 序列的酪氨酸 10 酚环上引入卤素原子会促进其在固态中的自组装。特别是，我们报告了两个卤素修饰序列的晶体结构，我们发现它们在固态中通过卤素介导的相互作用得到稳定。结构研究得到了非共价相互作用（NCI）分析的支持。我们的结果证明，选择性卤化氨基酸会增强原本无结构的生物相关序列的超分子组织。这种方法可能发展成为稳定高度多态肽区域的一般策略。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/da1abea91747/OPEN-9-253-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/8fdc53a01824/OPEN-9-253-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/0cf8263ea388/OPEN-9-253-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/858230532e40/OPEN-9-253-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/9c574ecbb492/OPEN-9-253-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/dd34b0f8f36f/OPEN-9-253-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/b68722d24685/OPEN-9-253-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/da1abea91747/OPEN-9-253-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/8fdc53a01824/OPEN-9-253-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/0cf8263ea388/OPEN-9-253-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/858230532e40/OPEN-9-253-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/9c574ecbb492/OPEN-9-253-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/dd34b0f8f36f/OPEN-9-253-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/b68722d24685/OPEN-9-253-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2369/7041548/da1abea91747/OPEN-9-253-g006.jpg

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Atomic resolution map of the soluble amyloid beta assembly toxic surfaces.
可溶性淀粉样β蛋白组装毒性表面的原子分辨率图谱。
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