Key Laboratory of Theoretical and Computational Photochemistry Ministry of Education, College of Chemistry, Beijing Normal University, Beijing, 100875, China.
Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470, Mülheim an der Ruhr, Germany.
Angew Chem Int Ed Engl. 2016 Feb 5;55(6):2067-72. doi: 10.1002/anie.201509622. Epub 2016 Jan 6.
Photoswitchable azobenzene cross-linkers can control the folding and unfolding of peptides by photoisomerization and can thus regulate peptide affinities and enzyme activities. Using quantum mechanics/molecular mechanics (QM/MM) methods and classical MM force fields, we report the first molecular dynamics simulations of the photoinduced folding and unfolding processes in the azobenzene cross-linked FK-11 peptide. We find that the interactions between the peptide and the azobenzene cross-linker are crucial for controlling the evolution of the secondary structure of the peptide and responsible for accelerating the folding and unfolding events. They also modify the photoisomerization mechanism of the azobenzene cross-linker compared with the situation in vacuo or in solution.
光致变色偶氮苯交联剂可以通过光异构化控制肽的折叠和展开，从而调节肽的亲和力和酶活性。我们使用量子力学/分子力学（QM/MM）方法和经典 MM 力场，首次报道了光诱导 FK-11 肽折叠和展开过程的分子动力学模拟。我们发现，肽与偶氮苯交联剂之间的相互作用对于控制肽二级结构的演变至关重要，并负责加速折叠和展开事件。与真空或溶液中的情况相比，它们还改变了偶氮苯交联剂的光致异构化机制。
