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Interaction between the antimicrobial peptide aurein 1.2 dimer with mannans
(Wiley-Blackwell, 2014-09-01)
Interaction between the antimicrobial peptide Aurein 1.2 dimer and mannans
(Springer, 2014-11-01)
We have previously described the structure and the ability of a dimeric analog of the antimicrobial peptide Aurein 1.2 to aggregate Candida albicans. In this study, circular dichroism and fluorescence spectroscopy data ...
Effect of dimerization on the mechanism of action of aurein 1.2
(2016-06-01)
The mechanism of action of antimicrobial peptides depends on physicochemical properties such as structure, concentration, and oligomerization. Here, we focused on the effect of dimerization on the mechanism of action of ...
Differential stability of aurein 1.2 pores in model membranes of two probiotic strains
(American Chemical Society, 2020-08)
Aurein 1.2 is an antimicrobial peptide from the skin secretion of an Australian frog. In the previous experimental work, we reported a differential action of aurein 1.2 on two probiotic strains Lactobacillus delbrueckii ...
Interaction between the antimicrobial peptide aurein 1.2 dimer with mannans
(Wiley-Blackwell, 2015)
Interaction between the antimicrobial peptide aurein 1.2 dimer with mannans
(Wiley-Blackwell, 2015)
A coarse-grained approach to studying the interactions of the antimicrobial peptides aurein 1.2 and maculatin 1.1 with POPG/POPE lipid mixtures
(Springer, 2018-08)
In the present work we investigated the differential interactions of the antimicrobial peptides (AMPs) aurein 1.2 and maculatin 1.1 with a bilayer composed of a mixture of the lipids 1-palmitoyl-2-oleoyl-sn-glycero-3-pho ...
Dimerization of aurein 1.2: Effects in structure, antimicrobial activity and aggregation of Cândida albicans cells
(2013-06-01)
Antimicrobial peptides (AMPs) are a promising solution to face the antibiotic-resistant problem because they display little or no resistance effects. Dimeric analogues of select AMPs have shown pharmacotechnical advantages, ...