Surface activity and structures of two fragments of the human antimicrobial LL-37

Dannehl, Claudia; Gutsmann, Thomas; Brezesinski, Gerald

doi:10.1016/j.colsurfb.2013.03.030

Cited by 19 publications

(31 citation statements)

References 52 publications

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“…The dichroic ratio of the amide I band is comparable for both peptides, indicating that both peptides adopt the same orientation when interacting with DPPG. But the values are slightly below the values expected for a complete -helix lying flat at the air/water interface [31].…”

Section: Interactions Of Ll-32 and Ll-20 With Un-compressed Monolayersmentioning

confidence: 62%

“…Both events are connected with the partial dehydration of the C=O groups. As shown in [31], LL-20 adopts a less distinct -helix with more contact to water. The stronger shift for LL-32/DPPG mixtures could be therefore explained by a deeper insertion of LL-32 compared to LL-20 or simply by the formation of a more perfect -helix in contact with DPPG.…”

Section: Interactions Of Ll-32 and Ll-20 With Un-compressed Monolayersmentioning

confidence: 92%

“…Peptides: The two fragments of LL-37, namely LL-20 and LL-32, were synthesized with C-terminal amidation by solid-phase peptide synthesis technique with an automatic peptide synthesizer (model 433 A; Applied Biosystems) on Rink amide resin according to the fastmoc synthesis protocol of the manufacturer, including the removal of the N-terminal Fmoc-group [31]. The peptide was cleaved from the resin and deprotected and with 90% trifluoroacetic acid (TFA), 5% anisole, 2% thioanisole, 3% dithiothreitol for 3 h at room temperature.…”

Section: Methodsmentioning

confidence: 99%

“…It was shown that the peptides differ drastically in their surface activity (equilibrium adsorption pressure). As concluded from CD spectra, both peptides are unstructured in bulk but exhibit different secondary structures when adsorbed to the air/buffer interface [31,32]. While LL-32 transforms into an -helix lying flat at the buffer surface, with a helix diameter of 17 Å, LL-20 adopts a partly unstructured conformation.…”

Section: Introductionmentioning

confidence: 93%

“…In a previous study, the surface activity and structures of two fragments (LL-20 and LL-32) of LL-37 at the soft liquid/air interface have been characterized [31]. It was shown that the peptides differ drastically in their surface activity (equilibrium adsorption pressure).…”

Section: Introductionmentioning

confidence: 99%

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Interactions of Two Fragments of the Human Antimicrobial Peptide LL-37 with Zwitterionic and Anionic Lipid Monolayers

Dannehl

Brezesinski

Möhwald

2014

Zeitschrift Für Physikalische Chemie

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The interactions of two fragments of the human antimicrobial LL-37 with lipid monolayers at the soft liquid/air interface have been characterized. To model the interaction with mammalian cell membranes, lipid monolayers composed of the zwitterionic DPPC and DOPC were used. To investigate the interaction with bacterial cell membranes, lipid monolayers of anionic DPPG and POPG were used. DPPC and DPPG exhibit a first-order phase transition from the disordered liquid to the ordered condensed state, whereas POPG and DOPC monolayers are in the fluid disordered state at all surface pressures studied. Therefore, the influence of the monolayer phase state on peptide-lipid interactions can be studied. To obtain insight into the peptide structure and their influence on phospholipid membranes, film balance measurements were coupled with surface sensitive Infrared Reflection-Absorption Spectroscopy (IRRAS). The results were compared to CD measurements in bulk. LL-32 is more surface active and can better intercalate into lipid monolayers than LL-20. Even though LL-32 has no cell-selectivity, our results show how the peptide interacts differently with zwitterionic compared to anionic membrane models. The interaction with DPPC monolayers is based on simple intercalation of the peptides between the lipid molecules. However, the peptides bind in a two-step process to DPPG monolayers, which results in a fluidization of the lipid film. This can be related to a membrane thinning.

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Section: Interactions Of Ll-32 and Ll-20 With Un-compressed Monolayersmentioning

confidence: 62%

Section: Interactions Of Ll-32 and Ll-20 With Un-compressed Monolayersmentioning

confidence: 92%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Interactions of Two Fragments of the Human Antimicrobial Peptide LL-37 with Zwitterionic and Anionic Lipid Monolayers

Dannehl

Brezesinski

Möhwald

2014

Zeitschrift Für Physikalische Chemie

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Unique features of human cathelicidinLL‐37

et al. 2015

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Cathelicidins are antimicrobial peptides produced by humans and animals in response to various pathogenic microbes. This review intends to provide a brief overview of the expression, structure, properties and function of human cathelicidin LL-37 which may be a therapeutic agent against a variety of bacterial and viral diseases, cancers, and hard-to-heal wounds. Cathelicidins act as a primary defense against bacteria and other pathogens in the case of inflammation. They are able to kill bacteria and fungi, inhibit and destroy bacterial biofilms, and possess antiviral and antiparasitics properties. They can also play a role in angiogenesis, wound healing, and the regulation of apoptosis. The host defense peptide LL-37 has emerged as a novel modulator of tumor growth and metastasis in carcinogenesis of various types of cancers. LL-37 is an antimicrobial peptide able of inducing various effects. It acts as an anti- and pro- inflammatory factor. Cathelicidins are able to directly and selectively destroy membranes of various microbes and cancer cells, but they do not attack normal cells. The role of cathelicidins in cancer is double-sided. They play an important role in killing cancer cells and may provide a new possibility for the development of cancer therapeutics. However, they also can participate in carcinogenesis. Due to its activity spectrum LL-37 could be applied in pharmacotherapy. Cathelicidin peptides could serve as a template for the development of modern anti-microbial and anti-viral drugs. LL-37 is an excellent candidate to develop into therapeutics for infected wounds.

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Enhancement of Osteogenic Induction by LL37 Modified with a Collagen-Binding Domain In Vitro and In Vivo

Lin

Chen

Quan

et al. 2021

Int J Pept Res Ther

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Surface activity and structures of two fragments of the human antimicrobial LL-37

Cited by 19 publications

References 52 publications

Interactions of Two Fragments of the Human Antimicrobial Peptide LL-37 with Zwitterionic and Anionic Lipid Monolayers

Interactions of Two Fragments of the Human Antimicrobial Peptide LL-37 with Zwitterionic and Anionic Lipid Monolayers

Unique features of human cathelicidinLL‐37

Enhancement of Osteogenic Induction by LL37 Modified with a Collagen-Binding Domain In Vitro and In Vivo

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