Enzyme-responsive micelle-vesicle transition: A new method for the reconstitution of trans-membrane protein to liposome

Kazunari Akiyoshi, Nobuyuki Morimoto, Akifumi Murota

Research output: Chapter in Book/Report/Conference proceedingConference contribution

1 Citation (Scopus)

Abstract

New enzyme-responsive micellar systems in which an enzymatic reaction controls the amphiphilicity of the surfactants were reported. The surfactants in our study consist of a short alkyl chain and a maltooligomer as a primer which can be synthesized enzymatically. In the presence of phosphorylase and α-D-glucose-1-phosphate (G1P), the elongation reaction of the saccharide chain proceeds from the non-reducing 4-OH terminus of the glucan chain. Amylose-primer surfactants (C12MP) where an alkyl group (C12) is linked to the reduced terminus of maltopentaose form micelles in water, which are dissociated upon the enzymatic elongation reaction of the sugar moiety. The micelle-to-vesicle transition of mixed lipid/ primer systems can be controlled by using this property. This new type of transition system can be used in the reconsititution of transmembrane proteins to liposome.

Original languageEnglish
Title of host publication2007 International Symposium on Micro-NanoMechatronics and Human Science, MHS
Pages91-95
Number of pages5
DOIs
Publication statusPublished - 2007 Dec 1
Externally publishedYes
Event2007 International Symposium on Micro-NanoMechatronics and Human Science, MHS - Nagoya, Japan
Duration: 2007 Nov 112007 Nov 14

Publication series

Name2007 International Symposium on Micro-NanoMechatronics and Human Science, MHS

Other

Other2007 International Symposium on Micro-NanoMechatronics and Human Science, MHS
CountryJapan
CityNagoya
Period07/11/1107/11/14

ASJC Scopus subject areas

  • Artificial Intelligence
  • Computer Networks and Communications
  • Human-Computer Interaction
  • Electrical and Electronic Engineering

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