Peptide—Lipid Interactions: Insights and Perspectives

Sanderson, John M.

doi:10.1002/chin.200521280

Cited by 18 publications

(21 citation statements)

References 81 publications

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“…It is generally accepted that peptide activity is not detergent-like [50] occurring by phospholipid displacement that changes in membrane fluidity and/or reductions in membrane barrier properties that subsequently lead to membrane disruption. As in other models, peptides initially bind to the membrane mainly via electrostatic interactions, carpeting the phospholipid bilayer [51].…”

Section: Permeabilization Mechanismsmentioning

confidence: 99%

Antimicrobial peptides: an overview of a promising class of therapeutics

Giuliani¹,

Pirri²,

Nicoletto³

2007

Open Life Sciences

457

459

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Antibiotic resistance is increasing at a rate that far exceeds the pace of new development of drugs. Antimicrobial peptides, both synthetic and from natural sources, have raised interest as pathogens become resistant against conventional antibiotics. Indeed, one of the major strengths of this class of molecules is their ability to kill multidrug-resistant bacteria. Antimicrobial peptides are relatively small (6 to 100 aminoacids), amphipathic molecules of variable length, sequence and structure with activity against a wide range of microorganisms including bacteria, protozoa, yeast, fungi, viruses and even tumor cells. They usually act through relatively non-specific mechanisms resulting in membranolytic activity but they can also stimulate the innate immune response. Several peptides have already entered pre-clinical and clinical trials for the treatment of catheter site infections, cystic fibrosis, acne, wound healing and patients undergoing stem cell transplantation. We review the advantages of these molecules in clinical applications, their disadvantages including their low in vivo stability, high costs of production and the strategies for their discovery and optimization.

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Section: Permeabilization Mechanismsmentioning

confidence: 99%

Antimicrobial peptides: an overview of a promising class of therapeutics

Giuliani¹,

Pirri²,

Nicoletto³

2007

Open Life Sciences

457

459

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“…5 A and B) with a degree of overlap with the positively-charged patch. Tyrosine, among other aromatic amino acids, has been demonstrated to occur with high probability in the interfacial region of membrane proteins (37)(38)(39), and in model systems has been shown to associate strongly with phospholipids (40). The functionality of the tyrosine residues has yet to be investigated, but the motif is conserved within all RSV Ms.…”

Section: Comparison Of Structures In Solution and In Crystalmentioning

confidence: 99%

Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction

Money

McPhee²,

Mosely³

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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The matrix protein (M) of respiratory syncytial virus (RSV), the prototype viral member of the Pneumovirinae (family Paramyxoviridae, order Mononegavirales), has been crystallized and the structure determined to a resolution of 1.6 Å. The structure comprises 2 compact ␤-rich domains connected by a relatively unstructured linker region. Due to the high degree of side-chain order in the structure, an extensive contiguous area of positive surface charge covering Ϸ600 Å 2 can be resolved. This unusually large patch of positive surface potential spans both domains and the linker, and provides a mechanism for driving the interaction of the protein with a negatively-charged membrane surface or other virion components such as the nucleocapsid. This patch is complemented by regions of high hydrophobicity and a striking planar arrangement of tyrosine residues encircling the C-terminal domain. Comparison of the RSV M sequence with other members of the Pneumovirinae shows that regions of divergence correspond to surface exposed loops in the M structure, with the majority of viral species-specific differences occurring in the N-terminal domain.CD ͉ crystal structure ͉ respiratory syncytial virus ͉ sequence alignment R espiratory syncytial virus (RSV) is the prototype member of the Pneumovirinae, a subfamily of the Paramyxoviridae (order Mononegavirales). Morphologically, the extracellular virion consists of a lipid bilayer envelope, within which are embedded 3 glycoproteins, 2 of which (F and G) are important in cell attachment and viral entry into target cells. The third, the SH protein, contributes to pathology in the host (1). Internally, virions contain helical nucleocapsids that consist of N protein tightly bound to the negative-sense nonsegmented genomic RNA. The nucleocapsid in turn is associated with components of the viral RNA-dependent RNA polymerase (L, P, M2-1, and M2-2 proteins), forming the holo-nucleocapsid (2-4). Between the holo-nucleocapsid and the outer envelope there is a layer of matrix protein (M), which is associated peripherally with the membrane (5). The other family members of the Mononegavirales (Rhabdoviridae, Filoviridae, and Bornaviridae) all subscribe to this basic arrangement of the virion, although the overall morphology can vary between the families. For example, Paramyxoviridae virions are pleiomorphic, whereas the Rhabdoviridae have a regular bullet shape structure, and the Filoviridae have a more filamentous shape. Extracellular RSV virions form by a budding process that occurs at the plasma membrane within specialized lipid domains (5, 6) and M appears to drive the final assembly process, which is the incorporation of the holo-nucleocapsid and initiation of the budding process (7,8). Before budding, there is a coordinated assembly of viral components; and it is evident that the glycoproteins and M proteins are important determinants of the location on the plasma membrane at which the virus buds (9). It is also possible that the interaction between M and the glycoproteins, possibly mediat...

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“…In particular, studying the interaction between biological membranes and synthetic or natural peptides which possess the ability of forming transmembrane nanopores, is vital to understanding the functioning of ion channels and antimicrobial peptides. The Singer-Nicholson model-representation of a lipid membranes served as a conceptual pillar in cell biology and biophysics, and provided an extremely useful paradigm for the investigation of biomembranes properties, which began to be viewed as dynamic environments with the potential to affect protein structure and function [1,2]. Among others, electric features of biological membranes endow them with subtle and highly sophisticated modes of physiological behavior.…”

Section: Introductionmentioning

confidence: 99%

pH modulation of transport properties of alamethicin oligomers inserted in zwitterionic-based artificial lipid membranes

Chiriac

Luchian

2007

Biophysical Chemistry

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To cite this version:Roxana Chiriac, Tudor Luchian. pH modulation of transport properties of alamethicin oligomers inserted in zwitterionic-based artificial lipid membranes. Biophysical Chemistry, Elsevier, 2007, 130 (3) This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. (i.e., 0.65, 2.08, 2.94, 7 and 10.1). Our data strongly support the paradigm of a pH-dependent variation of the surface and membrane dipole potential which, in conjunction with possible lateral pressure effects within the lipid membrane, lead to a non-monotonic modulation of the electrical conductance of alamethicin oligomers. As expected, pH modulation of transport properties through the alamethicin oligomer is more visible for narrower pores (that is, the 1 st conductive state) with slightly better cation selectivity as compared to larger oligomers. A C C E P T E D

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Peptide—Lipid Interactions: Insights and Perspectives

Cited by 18 publications

References 81 publications

Antimicrobial peptides: an overview of a promising class of therapeutics

Antimicrobial peptides: an overview of a promising class of therapeutics

Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction

pH modulation of transport properties of alamethicin oligomers inserted in zwitterionic-based artificial lipid membranes

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