Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Effects of a N-Maleimide-Derivatized Phosphatidylethanolamine on the Architecture and Properties of Lipid Bilayers

Uxue Ballesteros
ORCID logo ,
Emilio J Gonzalez-Ramirez
,
Igor De la Arada
ORCID logo ,
Jesús Sot
,
Asier Etxaniz
ORCID logo ,
Félix M. Goñi
* ORCID logo ,
Alicia Alonso
ORCID logo ,
Lidia Ruth Montes
Version 1 : Received: 23 October 2023 / Approved: 24 October 2023 / Online: 24 October 2023 (07:54:34 CEST)

A peer-reviewed article of this Preprint also exists.

Ballesteros, U.; González-Ramirez, E.J.; de la Arada, I.; Sot, J.; Etxaniz, A.; Goñi, F.M.; Alonso, A.; Montes, L.R. Effects of a N-maleimide-derivatized Phosphatidylethanolamine on the Architecture and Properties of Lipid Bilayers †. Int. J. Mol. Sci. 2023, 24, 16570. Ballesteros, U.; González-Ramirez, E.J.; de la Arada, I.; Sot, J.; Etxaniz, A.; Goñi, F.M.; Alonso, A.; Montes, L.R. Effects of a N-maleimide-derivatized Phosphatidylethanolamine on the Architecture and Properties of Lipid Bilayers †. Int. J. Mol. Sci. 2023, 24, 16570.

Abstract

N-maleimide-derivatized phospholipids are often used to facilitate protein anchoring to membranes. In autophagy studies, this is applied to the covalent binding of Atg8, an autophagy protein, to a phosphatidylethanolamine (PE) in the nascent autophagosome. However, the question remains on how closely the N-maleimide PE derivative (PE-mal) mimicks the native PE in the bilayer. In the present paper, spectroscopic and calorimetric techniques have been applied to vesicles containing either PE or PE-mal (together with other phospholipids) to compare the properties of the native and derivatized forms of PE. According to differential scanning calorimetry, and to infrared spectroscopy, the presence of PE-mal did not perturb the fatty acyl chains in the bilayer. Fluorescence spectroscopy and microscopy showed that PE-mal did not alter bilayer permeability either. However, fluorescence emission polarization of Laurdan and DPH probes indicated an increased order, or decreased fluidity, in the bilayers containing PE-mal. In addition, infrared spectral data from the phospholipid phosphate region revealed a PE-mal-induced conformational change of the polar heads, accompanied by an increased hydration. Globally considered, the results suggest that PE-mal would be a reasonable substitute for PE in model membranes containing reconstituted proteins.

Keywords

maleimide; membrane fluidity; differential scanning calorimetry; fluorescence; infrared spectroscopy; autophagy proteins

Subject

Biology and Life Sciences, Biophysics

Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Download PDF Download Supplementary

Comments (0)

We encourage comments and feedback from a broad range of readers. See criteria for comments and our Diversity statement.

Leave a public comment
Send a private comment to the author(s)
* All users must log in before leaving a comment
Views 0
Downloads 0
Comments 0
Metrics 0
Get PDF Supplementary Files Cite Share 0
Bookmark BibSonomy Mendeley Reddit Delicious
×
Alerts
Notify me about updates to this article or when a peer-reviewed version is published.
We use cookies on our website to ensure you get the best experience.
Read more about our cookies here.