Functional characterization of pediocin PA-1 binding to liposomes in the absence of a protein receptor and its relationship to a predicted tertiary structure

Article Abstract:

Pediocin PA-1, a bacteriocin, binds to and causes the efflux of carboxyfluorescein (CF) from vesicles composed of lipids isolated from Listeria monocytogenes. Protein receptors are unnecessary for the CF efflux, as the vesicles lack membrane proteins. The efflux is higher in acidic conditions, and is dependent on the lipid and pediocin levels. Pediocin PA-1 also permeabilizes vesicles made of phosphatidylcholine. It probably contains two beta-sheets in a hairpin conformation that is stabilized by a disulfide bridge. Pediocin PA-1 contains regions of positively charged amino acids.

Observations, Protein binding, Molecular structure, Bacterial proteins

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Electrostatic interactions, but not the YGNGV consensus motif, govern the binding of pediocin PA-1 and its fragments to phospholipid vesicles

Article Abstract:

A research was conducted to investigate the binding of pediocin PA-1 and its fragments to target membranes utilizing tryptophan fluorescence as a probe, and the relationship between pediocin PA-1's structure and function. A membrane model system was utilized to study pediocin binding. Results showed that the mechanism for the initial binding step involved electrostatic interactions between positive patches of amino acid residues in the pediocin molecules and negatively charged phospholipid head groups in the target membrane.

Phospholipids, Electrostatics, Tryptophan

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Influence of lipid composition on pediocin PA-1 binding to phospholipid vesicles

Article Abstract:

Research was conducted to examine the effects of lipid composition on the initial binding step of Pediocin PA-1 to phospholipid vesicles and to find further evidence to support the electrostatic interaction model. Results reveal that the binding of pediocin PA-1 to the membrane strongly depended on the negative charge on the membrane surface. Findings provide the first evidence that the initial binding step for pediocin PA-1 exhibits a similar anionic lipid dependency.

Fatty acids, Lipids, Liposomes, Unsaturated fatty acids, Lipid synthesis

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