Cationic Pillar[6]arene Induces Cell Apoptosis by Inhibiting Protein Tyrosine Phosphorylation Via Host-Guest Recognition

We reported for the first time that cationic pillar[6]arene (cPA6) could tightly bind to peptide polymer (MW~20-50 kDa), an artificial substrate for tyrosine (Tyr) phosphorylation, and efficiently inhibit Tyr protein phosphorylation through host-guest recognition. We synthesized a nanocomposite of b...

Full description

Saved in:

Bibliographic Details
Published in:	International journal of molecular sciences 2020-07, Vol.21 (14), p.4979
Main Authors:	Li, Can-Peng, Lu, Yu-Xun, Zi, Cheng-Ting, Zhao, Yu-Ting, Zhao, Hui, Zhang, Ya-Ping
Format:	Article
Language:	eng
Subjects:	Antineoplastic Agents - administration & dosage Antineoplastic Agents - pharmacology Apoptosis Apoptosis - drug effects Aqueous solutions Binding sites Cations Cations - administration & dosage Cations - pharmacology Cell proliferation Drug Carriers - chemistry Enzymes Hep G2 Cells Humans Hydrocarbons Kinases Microscopy molecular recognition Nanocomposites Nanomaterials Nanostructures - chemistry Neoplasms - drug therapy Neoplasms - metabolism NMR Nuclear magnetic resonance Peptides Phosphorus Phosphorus - chemistry Phosphorylation Phosphorylation - drug effects pillararene Polymers protein tyrosine phosphorylation Proteins Quaternary Ammonium Compounds - administration & dosage Quaternary Ammonium Compounds - pharmacology Recognition Tumor cells Tyrosine Tyrosine - metabolism
Online Access:	Get full text
Tags:	Add Tag No Tags, Be the first to tag this record!

Description
Summary:	We reported for the first time that cationic pillar[6]arene (cPA6) could tightly bind to peptide polymer (MW~20-50 kDa), an artificial substrate for tyrosine (Tyr) phosphorylation, and efficiently inhibit Tyr protein phosphorylation through host-guest recognition. We synthesized a nanocomposite of black phosphorus nanosheets loaded with cPA6 (BPNS@cPA6) to explore the effect of cPA6 on cells. BPNS@cPA6 was able to enter HepG2 cells, induced apoptosis, and inhibited cell proliferation by reducing the level of Tyr phosphorylation. Furthermore, BPNS@cPA6 showed a stronger ability of inhibiting cell proliferation in tumor cells than in normal cells. Our results revealed the supramolecular modulation of enzymatic Tyr phosphorylation by the host-guest recognition of cPA6.
ISSN:	1422-0067 1661-6596 1422-0067