Antivesiculation and Complete Unbinding of Tail-Tethered Lipids

Published

January 8, 2024

Author(s)

Kuo-Chih Shih, Geoffray Leriche, Chung-Hao Liu, Jibao He, Vijay John, John Barker, Michihiro Nagao, Lin Yang, Jerry Yang, Mu-Ping Nieh

Abstract

We report the effect of tail-tethering on vesiculation and complete unbinding of bilayered membranes. Amphiphilic molecules of a bolalipid, resembling the tail-tethered molecular structure of archaeal lipids, with two identical zwitterionic phosphatidylcholine headgroups self-assemble into a large flat lamellar membrane, in contrast to the multilamellar vesicles (MLVs) observed in its counterpart, monopolar nontethered zwitterionic lipids. The antivesiculation is confirmed by smallangle X-ray scattering (SAXS) and cryogenic transmission electron microscopy (cyro-TEM). With the net charge of zero and higher bending rigidity of the membrane (confirmed by neutron spin echo (NSE) spectroscopy), the current membrane theory would predict that membranes should stack with each other (aka "bind") due to dominant van der Waals attraction, while the outcome of the nonstacking ("unbinding") membrane suggests that the theory needs to include entropic contribution for the nonvesicular structures. This report pioneers an understanding of how the tail-tethering of amphiphiles affects the structure, enabling better control over the final nanoscale morphology.

Citation

Langmuir

Volume

40

Issue

3

Pub Type

Journals

Download Paper

https://doi.org/10.1021/acs.langmuir.3c02663

Local Download

Keywords

lipid, unbinding, tail-tethering effect, small-angle x-ray scattering, neutron spin echo

Citation

Shih, K. , Leriche, G. , Liu, C. , He, J. , John, V. , Barker, J. , Nagao, M. , Yang, L. , Yang, J. and Nieh, M. (2024), Antivesiculation and Complete Unbinding of Tail-Tethered Lipids, Langmuir, [online], https://doi.org/10.1021/acs.langmuir.3c02663, https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=932014 (Accessed December 4, 2025)