Amyloid formation by short peptides in the presence of dipalmitoylphosphatidylcholine membranes

Gerbelli, B. B. ORCID: https://orcid.org/0000-0001-9300-8463, Oliveira, C. L. P. ORCID: https://orcid.org/0000-0002-3426-6507, Silva, E. R. ORCID: https://orcid.org/0000-0001-5876-2276, Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926 and Alves, W. A. ORCID: https://orcid.org/0000-0002-8394-2751 (2020) Amyloid formation by short peptides in the presence of dipalmitoylphosphatidylcholine membranes. Langmuir, 36 (48). pp. 14793-14801. ISSN 0743-7463 doi: 10.1021/acs.langmuir.0c02760

Abstract/Summary

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 β-sheet-rich 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.

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/94834
Identification Number/DOI	10.1021/acs.langmuir.0c02760
Refereed	Yes
Divisions	Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Publisher	American Chemical Society
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