1. Dynamics of lipid layers with/without bounded antimicrobial peptide halictine-1.
- Author
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Tesař, Adam, Jr.Kopecký, Vladimír, Kočišová, Eva, and Bednárová, Lucie
- Subjects
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PEPTIDE drugs , *PHOSPHOLIPIDS , *ANTI-infective agents , *PHOSPHOCHOLINE , *MIXTURES , *FOURIER transform infrared spectroscopy - Abstract
Dynamic behavior during the drying process of phospholipid multilayers composed of 1,2-dipalmitoyl- sn - glycero -3-phosphocholine and 1,2-dihexadecanoyl- sn -glycero-3-phospho-(1′-rac-glycerol) in mixtures of 1:4, was investigated by means of attenuated total reflection (ATR) Fourier transform infrared spectroscopy (FTIR). The interaction of the antimicrobial peptide halictine-1 (HAL-1), a linear dodecapeptide isolated from the venom of eusocial bee Halictus sexcinctus , with the lipid layer and its influence on the dynamics of the lipid layer was also studied. Analysis of ATR-FTIR spectra of the drying process by principal component analysis (PCA) clearly showed the sensitivity of C O vibrations at 1737 cm −1 , PO 2 vibrations in the region 1000–1250 cm −1 and CH stretching vibrations at 2850 and 2950 cm −1 to the hydration of the lipid layer. Nevertheless, PCA revealed that the lipid layers periodically oscillate between dehydration/hydration states. The protective influence of HAL-1 on the lipid layer, including the disappearance of dehydration/hydration oscillations, and slowing down of the drying of the system in the presence of the peptide was observed. PCA indicates a two-stage process of the interaction of HAL-1 with lipid layers and as well as the influence of HAL-1 on vibrations of the C O and PO 2 of lipid groups, whereas CH 2 and CH 3 vibrations remain intact during the binding of the peptide. The peptide binds to phospholipid head groups, changes its structure from a random coil to an α-helix structure, and interacts with the C O groups of the lipids, staying on the surface of the membrane. [ABSTRACT FROM AUTHOR]
- Published
- 2017
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