College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou 215123, China.
State Key Laboratory of Radiation Medicine and Protection, School for Radiological and Interdisciplinary Sciences (RAD-X), Soochow University, Suzhou, 215123, China.
J Mater Chem B. 2022 May 18;10(19):3716-3722. doi: 10.1039/d2tb00375a.
Modulating enzyme activities or functionalities is one of the primary features of biological systems, which is, however, a great challenge for artificial enzyme systems. In this work, we designed and synthesized a series of self-assembling peptides from histidine and other amino acids (Asp, Ser, Lys or Arg), which exist in the active site of natural enzymes. These peptides could undergo a conformational transition from random coils to β-sheet structures under physiological conditions and formed self-assembled nanotubes with obvious hydrolase activities. After incorporation of transition metal ions such as Cu, these peptides could coordinate with Cu ions, switch molecular conformations, and self-assemble into hybrid nanomaterials with altered morphologies and peroxidase-like activities. This work illustrates a facile approach for constructing artificial enzymes from self-assembling peptides with histidine residues whose catalytic functions could be modulated by incorporation of Cu ions.
调节酶的活性或功能是生物系统的主要特征之一，但这对于人工酶系统来说是一个巨大的挑战。在这项工作中，我们设计并合成了一系列由组氨酸和其他氨基酸（天冬氨酸、丝氨酸、赖氨酸或精氨酸）组成的自组装肽，这些氨基酸存在于天然酶的活性部位。这些肽在生理条件下可以从无规线团结构转变为β-折叠结构，并形成具有明显水解酶活性的自组装纳米管。在加入过渡金属离子如铜离子后，这些肽可以与铜离子配位，改变分子构象，并自组装成具有改变形态和过氧化物酶样活性的杂化纳米材料。这项工作说明了一种从含有组氨酸残基的自组装肽构建人工酶的简便方法，其催化功能可以通过加入铜离子来调节。
