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Side-chain amino acid based cationic polymer induced actin polymerizationElectronic supplementary information (ESI) available: Additional figures as noted in the text. See DOI: 10.1039/c6tb02814d

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 no...

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Bibliographic Details
Main Authors: Maiti, Binoy, Dutta, Priyanka, Seal, Soma, Pal, Sunirmal, De, Priyadarsi, Maiti, Sankar
Format: Article
Language:English
Online Access:Get full text
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Summary: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(NH 3 + -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 . A side-chain amino acid (alanine) based cationic polymer is able to nucleate, polymerize and stabilize actin filaments in vitro and in vivo .
ISSN:2050-750X
2050-7518
DOI:10.1039/c6tb02814d