English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Generation of bilayer asymmetry and membrane curvature by the sugar-cleaving enzyme invertase

Nowbagh, A., Deshwal, A., Kadu, M., Chaudhuri, A., Maiti, S., Lipowsky, R., et al. (2023). Generation of bilayer asymmetry and membrane curvature by the sugar-cleaving enzyme invertase. ChemSystemsChem, 5(2): e202200027. doi:10.1002/syst.202200027.

Item is

Files

show Files
hide Files
:
Article.pdf (Publisher version), 2MB
Name:
Article.pdf
Description:
-
OA-Status:
Hybrid
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-

Locators

show

Creators

show
hide
 Creators:
Nowbagh, Abhimanyu, Author
Deshwal, Akshi, Author
Kadu, Mayur, Author
Chaudhuri, Abhishek, Author
Maiti, Subhabrata, Author
Lipowsky, Reinhard1, Author                 
Bhatia, Tripta, Author
Affiliations:
1Reinhard Lipowsky, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863327              

Content

show
hide
Free keywords: Invertase; membrane curvature; giant unilamellar vesicle; bilayer asymmetry; hydrolysis
 Abstract: The catalytic action of invertase generates bilayer asymmetry that stabilises membrane curvature.  The driving mechanism for the generation of membrane curvature by invertase is investigated using giant unilamellar vesicles (GUVs).  The invertase cleaves the sucrose in the exterior compartment, thereby creating a sugar asymmetry across the bilayer membrane  that is measured for GUV membranes consisting of the lipid Dioleoylphosphatidylcholine (DOPC). Finally, the advantage of this method  to control membrane curvature  and to stabilize multi-sphere morphologies is demonstrated.  The GUV system in the presence of invertase is beneficial as a tool to generate multiple on-demand compartments with more  extended stability after the enzymatic activity has established the asymmetry.

Details

show
hide
Language(s): eng - English
 Dates: 2022-11-072023
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1002/syst.202200027
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: ChemSystemsChem
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 5 (2) Sequence Number: e202200027 Start / End Page: - Identifier: Other: 2570-4206