Themed collection Peptide-membrane interactions

20 items
Paper

The impact of antibacterial peptides on bacterial lipid membranes depends on stage of growth

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.

Graphical abstract: The impact of antibacterial peptides on bacterial lipid membranes depends on stage of growth
From the themed collection: Peptide-membrane interactions
Open Access Paper

Peptide lipidation in lysophospholipid micelles and lysophospholipid-enriched membranes

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.

Graphical abstract: Peptide lipidation in lysophospholipid micelles and lysophospholipid-enriched membranes
From the themed collection: Peptide-membrane interactions
Open Access Paper

Interactions of polymyxin B with lipopolysaccharide-containing membranes

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

Graphical abstract: Interactions of polymyxin B with lipopolysaccharide-containing membranes
From the themed collection: Peptide-membrane interactions
Paper

Lipid distributions and transleaflet cholesterol migration near heterogeneous surfaces in asymmetric bilayers

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.

Graphical abstract: Lipid distributions and transleaflet cholesterol migration near heterogeneous surfaces in asymmetric bilayers
From the themed collection: Peptide-membrane interactions
Paper

Membrane electrostatics sensed by tryptophan anchors in hydrophobic model peptides depends on non-aromatic interfacial amino acids: implications in hydrophobic mismatch

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

Graphical abstract: Membrane electrostatics sensed by tryptophan anchors in hydrophobic model peptides depends on non-aromatic interfacial amino acids: implications in hydrophobic mismatch
From the themed collection: Peptide-membrane interactions
Paper

Order-disorder transitions of cytoplasmic N-termini in the mechanisms of P-type ATPases

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

Graphical abstract: Order-disorder transitions of cytoplasmic N-termini in the mechanisms of P-type ATPases
From the themed collection: Peptide-membrane interactions
Paper

Controllable membrane remodeling by a modified fragment of the apoptotic protein Bax

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.

Graphical abstract: Controllable membrane remodeling by a modified fragment of the apoptotic protein Bax
From the themed collection: Peptide-membrane interactions
Paper

Caveolin induced membrane curvature and lipid clustering: two sides of the same coin?

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

Graphical abstract: Caveolin induced membrane curvature and lipid clustering: two sides of the same coin?
From the themed collection: Peptide-membrane interactions
Open Access Paper

Lipid specificity of the immune effector perforin

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

Graphical abstract: Lipid specificity of the immune effector perforin
From the themed collection: Peptide-membrane interactions
Paper

Molecular interactions of the M and E integral membrane proteins of SARS-CoV-2

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.

Graphical abstract: Molecular interactions of the M and E integral membrane proteins of SARS-CoV-2
From the themed collection: Peptide-membrane interactions
Paper

Estimating the accuracy of the MARTINI model towards the investigation of peripheral protein–membrane interactions

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.

Graphical abstract: Estimating the accuracy of the MARTINI model towards the investigation of peripheral protein–membrane interactions
From the themed collection: Peptide-membrane interactions
Paper

Modulation of a host’s cell membrane nano-environment by mycobacterial glycolipids: involvement of PI(4,5)P2 signaling lipid?

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.

Graphical abstract: Modulation of a host’s cell membrane nano-environment by mycobacterial glycolipids: involvement of PI(4,5)P2 signaling lipid?
From the themed collection: Peptide-membrane interactions
Paper

Structural changes in the model of the outer cell membrane of Gram-negative bacteria interacting with melittin: an in situ spectroelectrochemical study

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

Graphical abstract: Structural changes in the model of the outer cell membrane of Gram-negative bacteria interacting with melittin: an in situ spectroelectrochemical study
From the themed collection: Peptide-membrane interactions
Paper

Antimicrobial peptides: mechanism of action and lipid-mediated synergistic interactions within membranes

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.

Graphical abstract: Antimicrobial peptides: mechanism of action and lipid-mediated synergistic interactions within membranes
From the themed collection: Peptide-membrane interactions
Open Access Paper

Antimicrobial peptide activity in asymmetric bacterial membrane mimics

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.

Graphical abstract: Antimicrobial peptide activity in asymmetric bacterial membrane mimics
From the themed collection: Peptide-membrane interactions
Paper

Bcl-xL inhibits tBid and Bax via distinct mechanisms

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

Graphical abstract: Bcl-xL inhibits tBid and Bax via distinct mechanisms
From the themed collection: Peptide-membrane interactions
Open Access Accepted Manuscript - Paper

Virus-inspired designs of antimicrobial nanocapsules

From the themed collection: Peptide-membrane interactions
Open Access Accepted Manuscript - Paper

Mechanics of ESCRT-III mediated membrane fission

From the themed collection: Peptide-membrane interactions
Accepted Manuscript - Paper

Impact of Antimicrobial Peptides on E.coli-mimicking Lipid Model Membranes: correlating structural and dynamic effects using scattering methods

From the themed collection: Peptide-membrane interactions
Open Access Accepted Manuscript - Paper

The influence of phosphatidylserine localisation and lipid phase on membrane remodelling by the ESCRT-II/ESCRT-III complex

From the themed collection: Peptide-membrane interactions
20 items

About this collection

We are delighted to share with you a selection of the papers associated with a Faraday Discussion on Peptide-membrane interactions. More information about the event may be found here: http://rsc.li/peptide-fd2020. Additional articles will be added to the collection as they are published. The final versions of all the articles presented and a record of the live discussions will be published after the event.

It is difficult to overstate the importance of improving our understanding of how macromolecules such as peptides interact with membranes as this is such a fundamental aspect of how living systems operate. These processes are involved in protein folding, cell signalling, biogenesis, morphogenesis, disease and medical therapy. Next-generation synthetic biology goals will require a clearer understanding of how to control reticulated membrane structures in order to fabricate the supramolecular structures necessary for advanced synthesis and behaviour.

The molecular questions that require clarification and their solutions bridge the many divides between the fundamental physical chemistry of macromolecular polyelectrolytes and the supramolecular chemistry of membrane assemblies related to cell biology as well as drug development and synthetic biology. This Discussion meeting will seek to establish a sound platform for further developments in this important field by addressing several related aspects of peptide interactions with membranes. It will consider model theoretical and experimental systems in order to define the ‘reaction space’ that is possible and where appropriate with relevance to fundamental questions in cell biology including how peptides and proteins behave within biological membranes

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