Issue 6, 2017

Side-chain amino acid based cationic polymer induced actin polymerization

Abstract

Actin filament dynamics is important for proper cellular functions and is controlled by hundreds of actin binding proteins inside the cells. There are several natural and synthetic compounds that are able to bind actin and alter the actin filament dynamics. Since the actin dynamics changes due to nonspecific electrostatic interactions between negatively charged actin and positively charged proteins, and natural or synthetic compounds, herein we report the synthesis of poly(tert-butyl carbamate (Boc)-L-alanine methacryloyloxyethyl ester) (P(Boc-Ala-HEMA)) homopolymer in a controlled fashion by the reversible addition–fragmentation chain transfer (RAFT) polymerization. Subsequent deprotection of the Boc groups in the homopolymer under acidic conditions resulted in a positively charged polymer with primary amine moieties at the side chains. This cationic polymer (P(NH3+-Ala-HEMA)), is able to nucleate actin in vitro. The cationic polymer and corresponding partially fluorescence tagged polymer are able to nucleate actin filament in vivo. These polymers are nontoxic to the cultured cells and also stabilize the filamentous actin in vitro.

Graphical abstract: Side-chain amino acid based cationic polymer induced actin polymerization

Supplementary files

Article information

Article type
Paper
Submitted
27 Oct 2016
Accepted
09 Jan 2017
First published
09 Jan 2017

J. Mater. Chem. B, 2017,5, 1218-1226

Side-chain amino acid based cationic polymer induced actin polymerization

B. Maiti, P. Dutta, S. Seal, S. Pal, P. De and S. Maiti, J. Mater. Chem. B, 2017, 5, 1218 DOI: 10.1039/C6TB02814D

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