Interaction of α-and β-Oligoarginine-Acids and Amides with Anionic Lipid Vesicles:  A Mechanistic and Thermodynamic Study†

Biochemistry ◽  
2006 ◽  
Vol 45 (18) ◽  
pp. 5817-5829 ◽  
Author(s):  
Thomas Hitz ◽  
Rico Iten ◽  
James Gardiner ◽  
Kenji Namoto ◽  
Peter Walde ◽  
...  
2016 ◽  
Vol 1864 (9) ◽  
pp. 1206-1214 ◽  
Author(s):  
Manuela Pantusa ◽  
Brian Vad ◽  
Ove Lillelund ◽  
Lars Kjær ◽  
Daniel Otzen ◽  
...  

Author(s):  
Natália Bueno Leite ◽  
Dayane dos Santos Alvares ◽  
Bibiana Monson de Souza ◽  
Mário Sérgio Palma ◽  
João Ruggiero Neto

Membranes ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 307
Author(s):  
Dayane dos Santos Alvares ◽  
Ingrid Bernardes Santana Martins ◽  
Taisa Giordano Viegas ◽  
Mario Sergio Palma ◽  
Alexandre Suman de Araujo ◽  
...  

Anionic lipid membrane electrostatic potential and solution pH can influence cationic peptide adsorption to these bilayers, especially those containing simultaneously acid and basic residues. Here, we investigate the effects of the pH solution on MP1 (IDWKKLLDAAKQIL-NH2) adsorption to anionic (7POPC:3POPG) lipid vesicles in comparison to its analog H-MP1, with histidines substituting lysines. We used the association of adsorption isotherms and constant pH molecular dynamic simulations (CpHMD) to explore the effects of membrane potential and pH on peptides’ adsorption on this lipid membrane. We analyzed the fluorescence and zeta potential adsorption isotherms using the Gouy–Chapman theory. In CpHMD simulations for the peptides in solution and adsorbed on the lipid bilayer, we used the conformations obtained by conventional MD simulations at a μs timescale. Non-equilibrium Monte Carlo simulations provided the protonation states of acidic and basic residues. CpHMD showed average pKa shifts of two to three units, resulting in a higher net charge for the analog than for MP1, strongly modulating the peptide adsorption. The fractions of the protonation of acidic and basic residues and the peptides’ net charges obtained from the analysis of the adsorption isotherms were in reasonable agreement with those from CpHMD. MP1 adsorption was almost insensitive to solution pH. H-MP1 was much more sensitive to partitioning, at acidic pH, with an affinity ten times higher than in neutral ones.


Author(s):  
Mohammad Abu Sayem Karal ◽  
Md. Kabir Ahamed ◽  
Urbi Shyamolima Orchi ◽  
Md. Towhiduzzaman ◽  
Marzuk Ahmed ◽  
...  

1998 ◽  
Vol 64 (9) ◽  
pp. 3530-3532 ◽  
Author(s):  
Yuhuan Chen ◽  
Richard D. Ludescher ◽  
Thomas J. Montville

ABSTRACT Pediocin PA-1 bound to anionic lipid vesicles with saturated or unsaturated fatty acid chains in a lipid concentration-dependent fashion. Little change in binding parameters was observed for zwitterionic lipid vesicles. Decreasing the anionic lipid content of the vesicles gave a higher relative dissociation constant for the peptide-lipid interactions and further supports the electrostatic interaction model of binding.


2016 ◽  
Vol 60 (8) ◽  
pp. 5051-5053 ◽  
Author(s):  
Tala O. Khatib ◽  
Heather Stevenson ◽  
Michael R. Yeaman ◽  
Arnold S. Bayer ◽  
Antje Pokorny

ABSTRACTThe cytoplasmic membrane ofStaphylococcus aureuscontains ∼20 mol% of the net cationic lipid lysyl-phosphatidylglycerol (LPG). Elevated fractions of LPG are associated with increased resistance to cationic antibiotics, including the lipopeptide daptomycin (DAP). Although the surface charge of the bacterial cytoplasmic membrane is altered by LPG, surface binding of DAP was found to be only moderately affected in anionic vesicles containing 20 mol% LPG. These results suggest that charge repulsion cannot fully explain LPG-mediated resistance to cationic peptides.


2010 ◽  
Vol 21 (5) ◽  
pp. 544-549 ◽  
Author(s):  
Jing Wei-Guo ◽  
Liu Chang-Wei ◽  
Tang Ji-Lin ◽  
Wu Zheng-Yan ◽  
Dong Shao-Jun ◽  
...  

Author(s):  
Uwe Lücken ◽  
Joachim Jäger

TEM imaging of frozen-hydrated lipid vesicles has been done by several groups Thermotrophic and lyotrophic polymorphism has been reported. By using image processing, computer simulation and tilt experiments, we tried to learn about the influence of freezing-stress and defocus artifacts on the lipid polymorphism and fine structure of the bilayer profile. We show integrated membrane proteins do modulate the bilayer structure and the morphology of the vesicles.Phase transitions of DMPC vesicles were visualized after freezing under equilibrium conditions at different temperatures in a controlled-environment vitrification system. Below the main phase transition temperature of 24°C (Fig. 1), vesicles show a facetted appearance due to the quasicrystalline areas. A gradual increase in temperature leads to melting processes with different morphology in the bilayer profile. Far above the phase transition temperature the bilayer profile is still present. In the band-pass-filtered images (Fig. 2) no significant change in the width of the bilayer profile is visible.


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