Combined QCM-D and EIS study of supported lipid bilayer formation and interaction with pore-forming peptides

Briand, Elisabeth David; Zäch, Michael; Svedhem, Sofia; Kasemo, Bengt Herbert; Petronis, Šarūnas

doi:10.1039/b918288h

Cited by 82 publications

(104 citation statements)

References 68 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1B I-IV ) changes in the properties of the bilayer during AMP flow and subsequent buffer wash. These changes are quantified by the change in frequency (⌬F) and change in dissipation (⌬D) of an oscillating silica sensor, which is a technique commonly reported in the literature (15,(27)(28)(29)(30)(31)(32). Here, kinetic information is generally used to determine the rates and number of observable stages involved in each mode of action of the AMPs, whereas equilibrium data are related to the final mechanistic changes of the SLB.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Mechanism of Four de Novo Designed Antimicrobial Peptides

Murray

Pearson

Aranjo

et al. 2016

Journal of Biological Chemistry

View full text Add to dashboard Cite

Edited by George CarmanAs pathogenic bacteria become resistant to traditional antibiotics, alternate approaches such as designing and testing new potent selective antimicrobial peptides (AMP) are increasingly attractive. However, whereas much is known regarding the relationship between the AMP sequence and potency, less research has focused on developing links between AMP properties, such as design and structure, with mechanisms. Here we use four natural AMPs of varying known secondary structures and mechanisms of lipid bilayer disruption as controls to determine the mechanisms of four rationally designed AMPs with similar secondary structures and rearranged amino acid sequences. Using a Quartz Crystal Microbalance with Dissipation, we were able to differentiate between molecular models of AMP actions such as barrel-stave pore formation, toroidal pore formation, and peptide insertion mechanisms by quantifying differential frequencies throughout an oscillating supported lipid bilayer. Barrel-stave pores were identified by uniform frequency modulation, whereas toroidal pores possessed characteristic changes in oscillation frequency throughout the bilayer. The resulting modes of action demonstrate that rearrangement of an amino acid sequence of the AMP resulted in identical overall mechanisms, and that a given secondary structure did not necessarily predict mechanism. Also, increased mass addition to Gram-positive mimetic membranes from AMP disruption corresponded with lower minimum inhibitory concentrations against the Gram-positive Staphylococcus aureus.All multicellular organisms such as animals and plants protect themselves against pathogenic microbes by producing antimicrobial peptides (AMPs) 2 that selectively disrupt bacterial cell membranes (1). Although they are enormously diverse, AMPs are mainly comprised of hydrophobic and cationic amino acids that are spatially organized along the molecule. Because bacteria depend on the integrity of their anionic cell membrane, disrupting their membrane with cationic peptides could offer an alternate strategy to conventional antibiotics for killing pathogenic bacteria (2). As these pathogens become resistant to traditional antibiotics, alternate approaches such as designing and testing new potent selective antimicrobial peptides are increasingly attractive.The proper composition of amino acids, their sequential arrangement, and peptide length are essential for effective action of AMPs (3). It has been demonstrated that AMP activity is more closely tied to amino acid composition than amino acid sequence or AMP structure (4 -8). However, it has recently been shown that for the ␣-helical class of AMPs, ordering amino acids during AMP design into an imperfect amphipathic ␣-helix, a helix barrel-stave with one hydrophobic and one hydrophilic face where the hydrophobic face is disrupted by one hydrophilic amino acid, is beneficial for increasing AMP activity (9). Understanding the mechanism behind how these peptides disrupt cell membranes could benefit future designs of p...

show abstract

Section: Resultsmentioning

confidence: 99%

“…Equilibrium Behavior-PG-1 has large negative values of ⌬⌬F (all overtones ϽϪ20 Hz) and a value of ⌬⌬F 3-9 o ϭ 9.1 Hz kDa Ϫ1 , indicating significant frequency decreases, a parameter change commonly related to increasing mass (31), throughout the SLB with a preference for interaction furthest from the sensor surface (Fig. 1B I ).…”

Section: ϫ6mentioning

confidence: 99%

Mechanism of Four de Novo Designed Antimicrobial Peptides

Murray

Pearson

Aranjo

et al. 2016

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…The coupling of biomimetic dynamic interfaces with electrochemical impedance spectroscopy has shown value in the study of ion transport studies across tethered bilayers [56]. Electrochemical impedance spectroscopy may prove valuable used in conjunction with the previously described techniques [57,58]. Again electrode construction with readily chemically adaptable surface materials such as gold, silver and glass/silica amongst others make this a promising approach for introducing functional interfaces.…”

Section: Electrochemical Sensing Platformsmentioning

confidence: 98%

Dynamic Nanoplatforms in Biosensor and Membrane Constitutional Systems

Mahon

Aastrup

Barboiu

2011

Constitutional Dynamic Chemistry

View full text Add to dashboard Cite

Molecular recognition in biological systems occurs mainly at interfacial environments such as membrane surfaces, enzyme active sites, or the interior of the DNA double helix. At the cell membrane surface, carbohydrate-protein recognition principles apply to a range of specific non-covalent interactions including immune response, cell proliferation, adhesion and death, cell-cell interaction and communication. Protein-protein recognition meanwhile accounts for signalling processes and ion channel structure. In this chapter we aim to describe such constitutional dynamic interfaces for biosensing and membrane transport applications. Constitutionally adaptive interfaces may mimic the recognition capabilities intrinsic to natural recognition processes. We present some recent examples of 2D and 3D constructed sensors and membranes of this type and describe their sensing and transport capabilities.

show abstract

“…The great potential of this multi-mode chip sensor lies in further to reveal complex biomolecule binding information during their interactions (such as molecule conformation [24], structure change [25,26] etc. ), which is rather difficult to be determined by a single measurement.…”

Section: Viscometric Response To Glucosementioning

confidence: 99%