Study at the Air/Water Interface of a Hepatitis A N-Acetylated and C-Amidated Synthetic Peptide (AcVP3(110–121)–NH2)

Sospedra, P.; Espina, Marta; Gómara, María J.; Alsina, M. A.; Haro, Isabel; Mestres, C.

doi:10.1006/jcis.2001.7899

Cited by 9 publications

(5 citation statements)

References 13 publications

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“…However, in the presence of AP1 (Table 3), positive values of Δ G Mix are observed for E. coli model membranes, indicating that, although the lipids forming these monolayers are miscible, repulsive interactions are established in the presence of the peptide, thereby decreasing membrane stability. These values of Δ G Mix become progressively more positive as surface pressure increases, showing that, at higher surface pressures, mutual interactions between the component molecules of these membranes are weaker than those occurring in monolayers formed by their pure components [43], becoming increasingly less stable with compression. This instability may contribute to the susceptibility of E. coli model membranes to the action of AP1.…”

Section: Resultsmentioning

confidence: 99%

Investigations into the ability of an oblique α‐helical template to provide the basis for design of an antimicrobial anionic amphiphilic peptide

et al. 2006

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AP1 (GEQGALAQFGEWL) was shown by theoretical analysis to be an anionic oblique-orientated alpha-helix former. The peptide exhibited a monolayer surface area of 1.42 nm(2), implying possession of alpha-helical structure at an air/water interface, and Fourier transform infrared spectroscopy (FTIR) showed the peptide to be alpha-helical (100%) in the presence of vesicle mimics of Escherichia coli membranes. FTIR lipid-phase transition analysis showed the peptide to induce large decreases in the fluidity of these E. coli membrane mimics, and Langmuir-Blodgett trough analysis found the peptide to induce large surface pressure changes in monolayer mimics of E. coli membranes (4.6 mN.m(-1)). Analysis of compression isotherms based on mixing enthalpy (DeltaH) and the Gibbs free energy of mixing (DeltaG(Mix)) predicted that these monolayers were thermodynamically stable (DeltaH and DeltaG(Mix) each negative) but were destabilized by the presence of the peptide (DeltaH and DeltaG(Mix) each positive). The peptide was found to have a minimum lethal concentration of 3 mm against E. coli and was seen to cause lysis of erythrocytes at 5 mm. In combination, these data clearly show that AP1 functions as an anionic alpha-helical antimicrobial peptide and suggest that both its tilted peptide characteristics and the composition of its target membrane are important determinants of its efficacy of action.

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Section: Resultsmentioning

confidence: 99%

Investigations into the ability of an oblique α‐helical template to provide the basis for design of an antimicrobial anionic amphiphilic peptide

et al. 2006

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“…The interaction of LAM, C 3 (CA) 2 , C 3 (OA) 2 , HTAB, and CHX with lipid monolayers was also investigated as the influence in the compression isotherms of DPPC, DPPG, and E. coli lipid extract. The isotherms taken from pure DPPC and DPPG (Figure a,b) showed the well-known phase transition from liquid-expanded (LE) to liquid-condensed (LC) phases around 7 mN m -1 and 90 Å 2 mol -1 of molecular area c) did not show the LE−LC transition, presumably because it was a mixture of three different phospholipids and contained 17% w/w of other unidentified compounds.…”

Section: Resultsmentioning

confidence: 99%

Interaction of Antimicrobial Arginine-Based Cationic Surfactants with Liposomes and Lipid Monolayers

et al. 2004

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The present work examines the relationship between the antimicrobial activity of novel arginine-based cationic surfactants and the physicochemical process involved in the perturbation of the cell membrane. To this end, the interaction of these surfactants with two biomembrane models, namely, 1,2-dipalmitoylsn-glycero-3-phosphocholine (DPPC) multilamellar lipid vesicles (MLVs) and monolayers of DPPC, 1,2dipalmitoyl-sn-glycero-3-[phospho-rac-(1-glycerol)] sodium salt (DPPG), and Escherichia coli total lipid extract, was investigated. For the sake of comparison, this study included two commercial antimicrobial agents, hexadecyltrimethylammonium bromide and chlorhexidine dihydrochloride. Changes in the thermotropic phase transition parameters of DPPC MLVs in the presence of the compounds were studied by differential scanning calorimetry analysis. The results show that variations in both the transition temperature (Tm) and the transition width at half-height of the heat absorption peak (∆T1/2) were consistent with the antimicrobial activity of the compounds. Penetration kinetics and compression isotherm studies performed with DPPC, DPPG, and E. coli total lipid extract monolayers indicated that both steric hindrance effects and electrostatic forces explained the antimicrobial agent-lipid interaction. Overall, in DPPC monolayers single-chain surfactants had the highest penetration capacity, whereas gemini surfactants were the most active in DPPG systems. The compression isotherms showed an expansion of the monolayers compared with that of pure lipids, indicating an insertion of the compounds into the lipid molecules. Owing to their cationic character, they are incorporated better into the negatively charged DPPG than into zwitterionic DPPC lipid monolayers.

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“…5 were also used to calculate the Gibbs free energy of mixing ( G Mix ). Table 3 shows that for both organisms, G Mix << RT = 2444.316 J mol -1 , indicating that deviations from ideal mixing behaviour in these model membranes are small (Sospedra et al, 2001). +200 to -100 on addition of VP1 (Fig.…”

Section: Vp1-lipid Compression Isotherms and Their Thermodynamic Analmentioning

confidence: 91%

The impact of membrane lipid composition on antimicrobial function of an α-helical peptide

Dennison

Morton

Harris

et al. 2008

Chemistry and Physics of Lipids

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Study at the Air/Water Interface of a Hepatitis A N-Acetylated and C-Amidated Synthetic Peptide (AcVP3(110–121)–NH2)

Cited by 9 publications

References 13 publications

Investigations into the ability of an oblique α‐helical template to provide the basis for design of an antimicrobial anionic amphiphilic peptide

Investigations into the ability of an oblique α‐helical template to provide the basis for design of an antimicrobial anionic amphiphilic peptide

Interaction of Antimicrobial Arginine-Based Cationic Surfactants with Liposomes and Lipid Monolayers

The impact of membrane lipid composition on antimicrobial function of an α-helical peptide

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