Premium
Targeted Polypeptide–Microtubule Aggregation with Cucurbit[8]uril for Enhanced Cell Apoptosis
Author(s) -
Zhang YingMing,
Liu JiangHua,
Yu Qilin,
Wen Xin,
Liu Yu
Publication year - 2019
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201903243
Subject(s) - supramolecular chemistry , microtubule , chemistry , peptide , in vivo , biophysics , apoptosis , in vitro , stereochemistry , biochemistry , microbiology and biotechnology , crystallography , biology , crystal structure
Tunable protein assemblies not only hold a dominant position in vital biological events but are also a significant theme in supramolecular chemistry. Herein, we demonstrated that the intertubular aggregation of microtubules (MTs) could be efficiently regulated by a synergistic polypeptide–tubulin interaction and host–guest complexation. The benzylimidazolium‐modified antimitotic peptide (BP) could recognize the MTs and concurrently form stable inclusion complexes with avirulent cucurbit[7]uril (CB[7]) and cucurbit[8]uril (CB[8]) in different binding stoichiometries. The self‐assembling morphology of MTs was converted from fibrous to nanoparticulate aggregates via extensive BP⊂CB[8] cross‐linkage, leading to significant cell apoptosis and tumor ablation in vivo. The targeted (BP⊂CB[8])@MT ternary assembly provides a facile supramolecular method to enhance the protein–protein interactions, which may be developed as a therapy for degenerative diseases, such as cancer.