Journal
LANGMUIR
Volume 36, Issue 48, Pages 14793-14801Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.langmuir.0c02760
Keywords
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Funding
- FAPESP [2017/02317-2, 2014/50867-3, 2018/05888-3, 2018/16092-5, 2017/27078-0, 2019/20907-7]
- CNPq [304389/2019-6, 465389/2014-7, 303001/2019-4]
- Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [18/16092-5, 14/50867-3, 17/27078-0, 18/05888-3] Funding Source: FAPESP
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The aggregation of two short peptides, [RF] and [RF](4) (where R = arginine and F = phenylalanine), at dipalmitoylphosphatidylcholine (DPPC) model membranes was investigated at the air-water interface using the Langmuir technique and vesicles in aqueous solutions. The molar ratio of the peptide and lipid components was varied to provide insights into the peptide-membrane interactions, which might be related to their cytotoxicity. Both peptides exhibited affinity to the DPPC membrane interface and rapidly adopted beta-sheetrich structures upon adsorption onto the surface of the zwitterionic membrane. Results from adsorption isotherm and small-angle X-ray scattering experiments showed changes in the structural and thermodynamic parameters of the membrane with increasing peptide concentration. Using atomic force microscopy, we showed the appearance of pores through the bilayer membranes and peptide aggregation at different interfaces, suggesting that the hydrophobic residues might have an effect on both pore size and layer structure, facilitating the membrane disruption and leading to different cytotoxicity effects.
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