Noncovalent Interactions with Proteins Modify the Physicochemical Properties of a Molecular Switch

被引：16

作者：

Amdursky, Nadav ^{[1
,2
]}

Kundu, Pintu K. ^{[1
]}

Ahrens, Johannes ^{[1
]}

Huppert, Dan ^{[3
]}

Klajn, Rafal ^{[1
]}

机构：

[1] Weizmann Inst Sci, Dept Organ Chem, IL-76100 Rehovot, Israel

[2] Weizmann Inst Sci, Dept Mat & Interfaces, IL-76100 Rehovot, Israel

[3] Tel Aviv Univ, Sch Chem, IL-69978 Tel Aviv, Israel

来源：

CHEMPLUSCHEM | 2016年 / 81卷 / 01期

基金：

欧洲研究理事会;

关键词：

molecular switches; photochromism; photoisomerization; solvatochromism; spiropyrans; BOVINE SERUM-ALBUMIN; ZIPPER CRYSTALLIZATION; MEROCYANINE ISOMERS; ELECTRON-TRANSPORT; ESCHERICHIA-COLI; ALPHA-AMYLASE; SPIROPYRAN; MECHANISM; LIGHT; PHOTOPHARMACOLOGY;

D O I：

10.1002/cplu.201500417

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

It is reported that spiropyrana widely investigated molecular photoswitchcan be stabilized in aqueous environments in the presence of a variety of proteins, including human serum albumin, insulin fibrils, lysozyme, and glucose oxidase. The optical properties of the complexed photoswitch are protein dependent, with human serum albumin providing the spiropyran with emission features previously observed for a photoswitch confined in media of high viscosity. Despite being bound to the protein molecules, spiropyran can undergo a ring-opening reaction upon exposure to UV light. This photoisomerization process can affect the properties of the proteins: here, it is shown that the electrical conduction through human serum albumin to which the spiropyran is bound increases following the ring-opening reaction.

引用

页码：44 / 48

页数：5

共 53 条

[1] Redox activity distinguishes solid-state electron transport from solution-based electron transfer in a natural and artificial protein: cytochrome C and hemin-doped human serum albumin [J].