Aß Amyloid Fibers Drastically Alter the Topography and Mechanical Properties of Lipid Membranes.
Langmuir
; 39(51): 18923-18934, 2023 12 26.
Article
em En
| MEDLINE
| ID: mdl-38079396
ABSTRACT
Alzheimer's disease (AD) is related to the fibrillation of the Aß peptides at neuronal membranes, a process that depends on the lipid composition and may impart different physical states to the membrane. In the present work, we study the properties of the Aß peptide when mixed with a zwitterionic lipid (DMPC), using the Langmuir monolayer technique as an approach to control membrane physical conditions. First, we build on previous characterizations of pure Aß monolayers and observe that, in addition to high shear, these films present a pronounced compressional hysteresis. When Aß is assembled with DMPC in a binary film, the resulting membranes become heterogeneous, with a peptide-enriched phase distributed in a network-like pattern, and they exhibit a lateral transition that depends on the Aß content. At lower peptide proportions, the films segregate into two well-defined phases one consisting of lipids and another enriched with peptides. The reflectivity of these phases differs from that obtained for pure Aß films. Thus, the formed fibers effectively cover most of the interface area and remain stable at higher pressures (from 20 to 30 mN m-1 depending on Aß content) compared to pure peptide films (17 mN m-1). Furthermore, such structures induce a compressional hysteresis in the film, similar to that of pure peptide films (which is nonexistent in the pure lipid monolayer), even at low peptide proportions. We claim that the mechanical properties at the interface are governed by the size of the fibril-like structures. Based on the low molar fractions and surface packing at which these phenomena were observed, we postulate that as a consequence of peptide intermolecular interactions, Aß may have drastic effects on the molecular arrangement and mechanical properties of a lipid membrane.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos beta-Amiloides
/
Fenômenos Mecânicos
/
Lipídeos de Membrana
Limite:
Humans
Idioma:
En
Revista:
Langmuir
Assunto da revista:
QUIMICA
Ano de publicação:
2023
Tipo de documento:
Article
País de afiliação:
Argentina