ArticleBiochimica et biophysica acta2010
A comparative study on the interactions of SMAP-29 with lipid monolayers.
Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Antibiofilm properties of cathelicidin LL-37: an in-depth review.World journal of microbiology & biotechnology · 2023Review
- Article
- Study of the Mechanism of the Antimicrobial Activity of Novel Water Soluble Ammonium Quaternary Benzanthrone on Model Membranes.The Journal of membrane biology · 2020Article
- Modulation of Endolysin LysECD7 Bactericidal Activity by Different Peptide Tag Fusion.Biomolecules · 2020Article
- Review
- Peptoid drug discovery and optimization via surface X-ray scattering.Biopolymers · 2019Review
- Cyclization Improves Membrane Permeation by Antimicrobial Peptoids.Langmuir : the ACS journal of surfaces and colloids · 2016Article
- Modification of Salmonella Lipopolysaccharides Prevents the Outer Membrane Penetration of Novobiocin.Biophysical journal · 2015Article
- Antimicrobial and biophysical properties of surfactant supplemented with an antimicrobial peptide for treatment of bacterial pneumonia.Antimicrobial agents and chemotherapy · 2015Article
- Guanidino groups greatly enhance the action of antimicrobial peptidomimetics against bacterial cytoplasmic membranes.Biochimica et biophysica acta · 2014Article
- Penetration of milk-derived antimicrobial peptides into phospholipid monolayers as model biomembranes.Biochemistry research international · 2013Article
- Mechanism of membrane perturbation by the HIV-1 gp41 membrane-proximal external region and its modulation by cholesterol.Biochimica et biophysica acta · 2012Article
- Cholesterol mediates membrane curvature during fusion events.Physical review letters · 2012Article
- Imaging interactions of cationic antimicrobial peptides with model lipid monolayers using X-ray spectromicroscopy.European biophysics journal : EBJ · 2011Article
- Role of the conformational rigidity in the design of biomimetic antimicrobial compounds.Angewandte Chemie (International ed. in English) · 2010Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
This work investigates the discrimination of lipid monolayers by the ovine antimicrobial peptide SMAP-29 and compares it to that of the human LL-37 peptide. Fluid phospholipid monolayers were formed in a Langmuir trough and subsequently studied with the X-ray scattering techniques of X-ray reflectivity and grazing incidence X-ray diffraction. Any changes in the phospholipid structure after injection of peptide under the monolayer were considered to be due to interactions between the peptides and lipids. The data show that SMAP-29 discriminates against negatively charged phospholipids in a similar way to LL-37. However, it is even more interesting to note that despite a higher concentration of SMAP-29 near the monolayer, ensured by its greater charge as compared to LL-37, the amount of SMAP-29 needed to observe monolayer disruption was around three and a half times the number of molecules of LL-37 used to see similar changes with the same system. This result suggests that the structure, amino acid sequence or size of the peptide may well be as important as electrical charge and therefore gives many implications for the further study of antimicrobial peptides with regards to novel drug design and development.
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