Antimicrobial peptides: an update on classifications and databases

A Bin Hafeez, X Jiang, PJ Bergen, Y Zhu - International journal of …, 2021 - mdpi.com
Antimicrobial peptides (AMPs) are distributed across all kingdoms of life and are an
indispensable component of host defenses. They consist of predominantly short cationic …

Membrane targeting cationic antimicrobial peptides

D Ciumac, H Gong, X Hu, JR Lu - Journal of colloid and interface science, 2019 - Elsevier
Many short cationic peptides are amphiphilic and are often termed antimicrobial peptides
(AMPs) as they can kill various microorganisms. These AMPs have largely been discovered …

[HTML][HTML] The human cathelicidin LL-37—A pore-forming antibacterial peptide and host-cell modulator

D Xhindoli, S Pacor, M Benincasa, M Scocchi… - … et Biophysica Acta (BBA …, 2016 - Elsevier
The human cathelicidin hCAP18/LL-37 has become a paradigm for the pleiotropic roles of
peptides in host defence. It has a remarkably wide functional repertoire that includes direct …

Effect of divalent cation removal on the structure of gram-negative bacterial outer membrane models

LA Clifton, MWA Skoda, AP Le Brun, F Ciesielski… - Langmuir, 2015 - ACS Publications
The Gram-negative bacterial outer membrane (GNB-OM) is asymmetric in its lipid
composition with a phospholipid-rich inner leaflet and an outer leaflet predominantly …

[HTML][HTML] Lipopolysaccharides at solid and liquid interfaces: models for biophysical studies of the gram-negative bacterial outer membrane

N Paracini, E Schneck, A Imberty, S Micciulla - Advances in Colloid and …, 2022 - Elsevier
Lipopolysaccharides (LPSs) are a constitutive element of the cell envelope of Gram-
negative bacteria, representing the main lipid in the external leaflet of their outer membrane …

The chemistry and biology of LL-37

MF Burton, PG Steel - Natural product reports, 2009 - pubs.rsc.org
Covering: up to June 2009LL-37 is a human host defence peptide that has a wide range of
biological functions, including antimicrobial and immunomodulatory properties. This review …

Structural Characterization of a Model Gram-Negative Bacterial Surface Using Lipopolysaccharides from Rough Strains of Escherichia coli

AP Le Brun, LA Clifton, CE Halbert, B Lin… - …, 2013 - ACS Publications
Lipopolysaccharides (LPS) make up approximately 75% of the Gram-negative bacterial
outer membrane (OM) surface, but because of the complexity of the molecule, there are very …

Salmonella Membrane Structural Remodeling Increases Resistance to Antimicrobial Peptide LL-37

MW Martynowycz, A Rice, K Andreev… - ACS infectious …, 2019 - ACS Publications
Gram-negative bacteria are protected from their environment by an outer membrane that is
primarily composed of lipopolysaccharides (LPSs). Under stress, pathogenic serotypes of …

Structural plasticity of LL-37 indicates elaborate functional adaptation mechanisms to bacterial target structures

K Zeth, E Sancho-Vaello - International Journal of Molecular Sciences, 2021 - mdpi.com
The human cathelicidin LL-37 is a multifunctional peptide of the human innate immune
system. Among the various functions of LL-37, its antimicrobial activity is important in …

Effects of specific versus nonspecific ionic interactions on the structure and lateral organization of lipopolysaccharides

C Jeworrek, F Evers, J Howe, K Brandenburg… - Biophysical journal, 2011 - cell.com
We report x-ray reflectivity and grazing incidence x-ray diffraction measurements of
lipopolysaccharide (LPS) monolayers at the water-air interface. Our investigations reveal …