Themed collection Peptide-membrane interactions

This article is based on the concluding remarks lecture given at the Faraday Discussion meeting on peptide–membrane interactions, held online, 8–10th September 2021. (Figure reproduced from Kratochvil et al., DOI: 10.1039/D1FD00061F).

Membrane–peptide interactions play critical roles in many cellular and organismal functions, including protection from infection, remodeling of membranes, signaling, and ion transport.

We use total internal reflection fluorescence microscopy combined with super-resolution tracking of multiple individual molecules, in order to create high-resolution maps of local membrane viscosity.

Biophysical and structural studies of peptide–lipid interactions, peptide topology and dynamics have changed our view of how antimicrobial peptides insert and interact with membranes.

We propose a novel approach to antimicrobial drug design that exploits the assembly of antimicrobial peptidic units in nanocapsules that can penetrate and rupture the bacterial membrane.

Acyl transfer to a membrane-associated peptide from both lysolipids and lipids occurs readily, leading to the generation of a lipidated peptide that adopts secondary structure in the absence of lipids.

Polymyxin B uses bacterial LPS as docking receptor to cross the outer membrane.

We report on the response of asymmetric lipid membranes composed of palmitoyl oleoyl phosphatidylethanolamine and palmitoyl oleoyl phosphatidylglycerol, to interactions with the frog peptides L18W-PGLa and magainin 2 (MG2a), as well as the lactoferricin derivative LF11-215.

Living organisms are separated from their environment by an interface/surface. Herein I discuss principles by which living surfaces deform.

Microsecond molecular dynamics simulations provide valuable insights into the aggregation patterns and membrane response around the M and E proteins of SARS-CoV-2. This work highlights the complex lipid–protein interactions during early viral assembly.

Varied lipid localization and cholesterol flipping dynamics were observed around different membrane-embedded entities, suggesting that unique lipid environments may be recruited by specific proteins.

We investigate the contribution of membrane interfacial electrostatics in tryptophan-mediated responses of membrane proteins to hydrophobic mismatch.

Using X-rays and neutrons we address the effect of AMPs on structure and dynamics of lipids in bacterial model membranes.

Interplay between lipid clustering and curvature in plasma membrane mediated by caveolin-1: the direct and indirect effects.

Circular dichroism of an H⁺, K⁺-ATPase N-terminal peptide at varying trifluoroethanol concentrations is investigated, indicating that its secondary structure is environmentally sensitive.

In this article, we investigate the ability of the MARTINI CG force field, specifically the 3 open-beta version, to reproduce known experimental observations regarding the membrane binding behavior of 12 peripheral membrane proteins and peptides.

We strategically introduced glutamic acid residues into a short sequence of the Bax protein that constitutively creates membrane pores. The resulting BaxE5 achieves acidity-triggered membrane remodeling.

Physical membrane properties play a determining role in defining the sensitivity of membranes to the immune effector perforin.

ESCRT-II/III machinery generates intraluminal vesicles with liquid ordered membranes but requires liquid disordered membrane in the bud neck for efficiency.

Quantification of interactions and localization dynamics of Bcl-xL with tBid and Bax reveals differences in the mechanism of inhibition.

Structurally diverse mycobacterial lipids distinctly alter a host’s PI(4,5)P₂ membrane organization and co-localization with actin, impacting the plasma membrane–cytoskeletal interactions.

Impact of maculatin 1.1 on supported lipid bilayers (SLBs) derived from early growth phase (EGP) or stationary growth phase (SGP) E. coli lipid extracts, monitored by atomic force microscopy which images bilayer morphology in real time.

Molecular scale changes in Gram-negative bacteria model membranes exposed to physiological electric fields and interacting with melittin antimicrobial peptide are discussed.