Fourier transform infrared spectroscopic studies of the effect of calcium ions on phosphatidylserine

Dluhy, Richard A.; Cameron, David G.; Mantsch, Henry H.; Mendelsohn, Richard

doi:10.1021/bi00295a043

Cited by 171 publications

(141 citation statements)

References 44 publications

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“…Between 23°C (i.e., the T m of pure DMPG) and 33°C (the transition temperature of DMPG in the presence of pediocin), there is a dramatic narrowing and a shift of ϳ3 cm Ϫ1 of the (CAO) bands. Similar observations already were observed for DMPG and phosphatidylserine bilayers upon addition of divalent cations (13,21,28) or upon incubation at 2 to 4°C of saturated phosphatidylcholine and phosphatidylglycerol bilayers, which results in the formation of the so-called subgel phase (47). Such spectral features were attributed to immobilized and dehydrated carbonyl groups due to an isothermal crystallization of the phospholipid molecules.…”

Section: Resultssupporting

confidence: 80%

Binding of Pediocin PA-1 with Anionic Lipid Induces Model Membrane Destabilization

Gaussier

Lefèvre

Subirade

2003

Appl Environ Microbiol

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To obtain molecular insights into the action mode of antimicrobial activity of pediocin PA-1, the interactions between this bacteriocin and dimyristoylphosphatidylcholine (DMPC) or dimyristoylphosphatidylglycerol (DMPG) model membranes have been investigated in D 2 O at pD 6 by Fourier transform infrared spectroscopy. The interactions were monitored with respect to alteration of the secondary structure of pediocin, as registered by the amide I band, and phospholipid conformation, as revealed by the methylene s (CH 2 ) and carbonyl (CAO) stretching vibrations. The results show that no interaction between pediocin and DMPC occurs. By contrast, pediocin undergoes a structural reorganization in the presence of DMPG. Upon heating, pediocin self-aggregates, which is not observed for this pD in aqueous solution. The gel-to-crystalline phase transition of DMPG shifts to higher temperatures with a concomitant dehydration of the interfacial region. Our results indicate that pediocin is an extrinsic peptide and that its action mechanism may lie in a destabilization of the cell membrane.Pediocin PA-1 is a 44-amino-acid (molecular mass, 4,629 Da; pI, 9.6) (35) class IIa bacteriocin (38) produced by Pediococcus acidilactici PAC 1.0 and naturally found in fermented sausages (37) or other meat and vegetable fermentations (5). Its sequence is highly homologous to other class IIa bacteriocins (59). The N-terminal 20-amino-acid half of pediocin is in the majority of cases polar or cationic and highly conserved, with the consensus sequence Y3-G4-N5-G6-V7. The C-terminal half (residues A21 to C44) is much less polar and less conserved, containing a hypothetical hydrophobic membrane interaction domain. Two disulfide bonds stabilize the peptide structure, the one between the residues 24 and 44 accounting for its broad range of antimicrobial activity (17). Because of its specific antimicrobial activity against the foodborne psychrotrophic pathogen Listeria monocytogenes, pediocin PA-1 can potentially serve as a nontoxic food preservative to improve the quality, naturalness, and safety (55) of dairy and meat products.The data for Listeria innocua death induced by pediocin PA-1 reveal that its activity maximum is reached near pD 6 and decreases at pD 7 and 8 (15, 30). A relation between activity and structure alterations has not yet been completely established. The loss of activity as a function of pD seems to be associated to a structural reorganization and a decrease in the protein flexibility that in turn results in an irreversible aggregation upon heating (30). The C-terminal region is first involved in the aggregation process, resulting in a total inactivation of the protein (30). The N-terminal region participates in the aggregation process in a second step. Pediocin can exist in a soluble and hydrophobic structural form (16). In an aqueous environment, pediocin presents an unordered structure as seen by circular dichroism (75) and Fourier transform infrared (FTIR) spectroscopy (30), whereas upon adsorption to vesicles, a structura...

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Section: Resultssupporting

confidence: 80%

Binding of Pediocin PA-1 with Anionic Lipid Induces Model Membrane Destabilization

Gaussier

Lefèvre

Subirade

2003

Appl Environ Microbiol

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“…A, spectrum b). These changes point at the dehydration of the phosphate group and the formation of a bidentate complex between the Ca 2+ ion and the phosphate ester [32].…”

Section: Citrate Removes Ca 2+ From Cochleate-surface Head Groupsmentioning

confidence: 99%

Dispersion and stabilization of cochleate nanoparticles

Bozó

Wacha

Mihály

et al. 2017

European Journal of Pharmaceutics and Biopharmaceutics

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Cochleates, calcium-stabilized membrane rolls of nanoscale diameter, promise a unique and efficient way of delivering lipid-soluble drugs, proteins or nucleic acids into biological systems because they protect the encapsulated material against enzymatic or chemical degradation. Self-aggregation, which typically arises during production and storage is a major obstacle that has so far precluded the development of an efficient cochleate-based drugdelivery system. Here we show that citric acid, added transiently in a narrow concentration range, effectively disperses cochleate aggregates, stabilizes the disperse state for long-term storage and preserves the canonical ultrastructure and topological characteristics of cochleate nanoparticles.

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“…8B) had an FT-IR spectrum similar to that seen with CHAPS. In both NCs there was a well defined peak at 1238 cm Ϫ1 characteristic of Ca 2ϩ bound to the O-P-O phosphodiester of the polar head group of PS (43).…”

Section: Fig 3 Sds-page Analysis Of the Proteins Present In Crmv Anmentioning

confidence: 99%

Physicochemical Characterization of the Nucleational Core of Matrix Vesicles

Genge

Dunkelberger

et al. 1997

Journal of Biological Chemistry

139

154

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While previous studies revealed that matrix vesicles (MV) contain a nucleational core (NC) that converts to apatite when incubated with synthetic cartilage lymph, the initial mineral phase present in MV is not well characterized. This study explored the physicochemical nature of this Ca 2؉ and P i -rich NC. MV, isolated from growth plate cartilage, were analyzed directly by solidstate 31 P NMR, or incubated with hydrazine or NaOCl to remove organic constituents. Other samples of MV were subjected to sequential treatments with enzymes, salt solutions, and detergents to expose the NC. We examined the NC using transmission electron microscopy, energy-dispersive analysis with x-rays, and electron and x-ray diffraction, Fourier transform-infrared spectroscopy, high performance thin-layer chromatographic analysis, and SDS-polyacrylamide gel electrophoresis. We found that most of the MV proteins and lipids could be removed without destroying the NC; however, NaOCl treatment annihilated its activity. SDS-polyacrylamide gel electrophoresis showed that annexin V, a phosphatidylserine (PS)-dependent Ca 2؉ -binding protein, was the major protein in the NC; high performance thin-layer chromatographic analysis revealed that the detergents removed the majority of the polar lipids, but left significant free cholesterol and fatty acids, and small but critical amounts of PS. Transmission electron microscopy showed that the NC was composed of clusters of ϳ1.0 nm subunits, which energy-dispersive analysis with x-rays revealed contained Ca and P i with a Ca/P ratio of 1.06 ؎ 0.01. Electron diffraction, x-ray diffraction, and Fourier transform-infrared analysis all indicated that the NC was noncrystalline.

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Fourier transform infrared spectroscopic studies of the effect of calcium ions on phosphatidylserine

Cited by 171 publications

References 44 publications

Binding of Pediocin PA-1 with Anionic Lipid Induces Model Membrane Destabilization

Binding of Pediocin PA-1 with Anionic Lipid Induces Model Membrane Destabilization

Dispersion and stabilization of cochleate nanoparticles

Physicochemical Characterization of the Nucleational Core of Matrix Vesicles

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