Lipase mimetic cyclodextrins.

Lipase mimetic cyclodextrins.
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脂肪酶模拟循环克罗斯特林。

DOI:
10.1039/d0sc05711h
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发表时间:
2020-11-19
期刊:
影响因子:
8.4
通讯作者:
Devaraj NK
Devaraj NK
中科院分区:
化学1区
文献类型:
--
作者:
Lee Y;Devaraj NK

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甘油磷脂(GPLs)在生物学中具有许多重要功能,包括形成细胞膜的关键结构组分和作为信号传导途径中的第二信使。开发能够检测特定GPL的仿生分子装置将能够调节GPL相关过程。然而,GPL的组成多样性,加上它们的疏水性,使得开发可以与特定脂质物质反应的合成支架具有挑战性。通过利用环糊精的主客体化学,我们设计了一种分子装置,可以在生理相关条件下选择性水解GPL。具有胺官能团的化学改性的α-环糊精显示出水解溶血-GPL,产生游离脂肪酸。当GPL脂质物质的混合物的一部分时,溶血GPL优先水解,并且反应效率取决于溶血GPL化学结构。这些发现为开发能够特异性操纵生命系统中脂质相关过程的分子装置奠定了基础。脂肪酶模拟环糊精(CD)可在生理相关条件下选择性水解天然溶血甘油磷脂(GPL)。
Glycerophospholipids (GPLs) perform numerous essential functions in biology, including forming key structural components of cellular membranes and acting as secondary messengers in signaling pathways. Developing biomimetic molecular devices that can detect specific GPLs would enable modulation of GPL-related processes. However, the compositional diversity of GPLs, combined with their hydrophobic nature, has made it challenging to develop synthetic scaffolds that can react with specific lipid species. By taking advantage of the host–guest chemistry of cyclodextrins, we have engineered a molecular device that can selectively hydrolyze GPLs under physiologically relevant conditions. A chemically modified α-cyclodextrin bearing amine functional groups was shown to hydrolyze lyso-GPLs, generating free fatty acids. Lyso-GPLs are preferentially hydrolyzed when part of a mixture of GPL lipid species, and reaction efficiency was dependent on lyso-GPL chemical structure. These findings lay the groundwork for the development of molecular devices capable of specifically manipulating lipid-related processes in living systems. Lipase mimetic cyclodextrins (CDs) can selectively hydrolyze native lyso-glycerophospholipids (GPLs) under physiologically relevant conditions.
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