RT Journal Article
T1 Impact of amylenes in dipeptide-mediated phospholipid vesicle integrity and aggregation
A1 Villanueva, Martín Eduardo
A1 Troncoso, Jacobo
A1 Losada Pérez, Patricia
A1 Jover Ramos, Aida
K1 Lipid vesicles
K1 Diphenylalanine
K1 Amylene
K1 Vesicle aggregation
K1 Model membrane organization
AB Interactions between lipid membranes are central to biological, biochemical, and biophysical processes. While adhesion between intact vesicles typically requires complex molecular linkers to overcome electrostatic and hydration repulsions, aggregation involves bilayer disruption and loss of vesicle integrity, a phenomenon more often associated with pathology. Here we report a minimal and straightforward route to induce aggregation of zwitterionic vesicles through the combined action of diphenylalanine (Phe-Phe), a dipeptide motif of the Alzheimer's β-amyloid peptide, and amylene, a small apolar alkene used as a chloroform stabilizer. Using NMR spectroscopy, microscopy, and thermodynamic and nanomechanical characterization, we demonstrate that Phe-Phe alone perturbs bilayer organization only mildly, but in the presence of amylene it synergistically drives membrane disruption and vesicle aggregation. These results highlight how the interplay of small molecules can reorganize zwitterionic membranes and eventually induce spontaneous aggregation.
PB Elsevier
SN 0167-7322
YR 2025
FD 2025
LK https://hdl.handle.net/10347/43141
UL https://hdl.handle.net/10347/43141
LA eng
NO Journal of Molecular Liquids Volume 437, Part C, 1 November 2025, 128596
NO Support from the Spanish Ministry of Science, Innovation, and Universities under Grants No. PID2020-115722GB-C22 and PID2023-147148NB-I00 are greatly acknowledged. Support from the project ‘DELTA’ with project number 40008129 by ‘Fonds de la Recherche Scientifique’ (FNRS). M.E.V is a Collaborateur Scientifique of the Fonds de la recherche scientifique- FNRS. A. J. acknowledges A. López Greco for his help in the model discussion.
DS Minerva
RD 24 abr 2026