Biomolecule surface patterning may enhance membrane association

TL;DR

This study models amphipathic proteins as patterned cylinders to understand how surface patterning influences membrane association, revealing that stripe thickness and bilayer properties significantly affect interaction thermodynamics.

Contribution

It introduces a thermodynamic model of membrane association based on patterned cylinders representing alpha-helical proteins, highlighting the role of surface patterning.

Findings

Stripe thickness controls free energy of membrane interaction.

Bilayer structure influences protein association.

Optimal stripe parameters can mimic protein-membrane binding.

Abstract

Under dehydration conditions, amphipathic Late Embryogenesis Abundant (LEA) proteins fold spontaneously from a random conformation into alpha-helical structures and this transition is promoted by the presence of membranes. To gain insight into the thermodynamics of membrane association we model the resulting alpha-helical structures as infinite rigid cylinders patterned with hydrophobic and hydrophilic stripes oriented parallel to their axis. Statistical thermodynamic calculations using Single Chain Mean Field (SCMF) theory show that the relative thickness of the stripes controls the free energy of interaction of the alpha-helices with a phospholipid bilayer, as does the bilayer structure and the depth of the equilibrium penetration of the cylinders into the bilayer. The results may suggest the optimal thickness of the stripes to mimic the association of such protein with membranes.