Wechselwirkungen zwischen amyloidogenen Proteinen und Membranen: Modellsysteme liefern mechanistische Einblicke

Abstract

Die Toxizität amyloidbildender Proteine ist mit ihrer Wechselwirkung mit Membranen korreliert. Bemerkenswerterweise führen Bindungsereignisse zwischen amyloidogenen Proteinen und Membranen beiderseits zu Strukturstörungen, die mit Toxizität assoziiert sind. Membranoberflächen vermitteln die Umwandlung amyloidbildender Proteine in toxische Aggregate, amyloidbildende Proteine wiederum beeinträchtigen die strukturelle Integrität der Zellmembran. Neuere Untersuchungen an künstlichen Modellmembranen haben eine bemerkenswerte Ähnlichkeit im Mechanismus der Membranpermeabilisierung von amyloidbildenden Proteinen, porenbildenden Toxinen und antimikrobiellen Peptiden aufgezeigt.

Maintenance of Amyloid β Peptide Homeostasis by Artificial Chaperones Based on Mixed‐Shell Polymeric Micelles

“…[8a] This result indicates that the progress of Ab fibrillation follows a typical nucleation-growth mode that consists of three stages: lag phase, elongation phase, and stationary phase. [15] The saturation of the ThT FI after approximately 90 h indicates that all of the Ab end up in the form of fibrils (also see Figure 2 c). Upon the introduction of MSPMs, the lag phase extended and the FI at saturation decreased, indicating that the MSPM-based chaperone can effectively suppress the Ab fibrillation process.…”

Cross‐Amyloid Interaction of Aβ and IAPP at Lipid Membranes

“…[9][10][11] Several studies have shown that lipid-peptide interactions can play a crucial role in amyloid formation of both IAPP and Ab, [1,3,[15][16][17][18][19][20][21][22][23][24][25][26][27][28] and the enhancement of fibrillation in the presence of membranes is believed to be causatively linked to the cellular damage caused by Ab or IAPP assemblies. [25,26,28] Here, the interaction of IAPP and Ab with a complex heterogeneous (raft-like) model biomembrane system comprising 15 % DOPC, 10 % DOPG, 40 % DPPC, 10 % DPPG, and 25 % cholesterol has been studied. This lipid system allows for addressing effects of lateral heterogeneity (i.e., coexisting liquid-disordered and liquid-ordered domains) as well as charge effects upon peptide-membrane interactions.…”

Electrodeposition of Single‐Metal Nanoparticles on Stable Protein 1 Membranes: Application of Plasmonic Sensing by Single Nanoparticles

“…[1] Biological membranes supported on substrates are widely used to mimic the dynamics and structural features of cell membranes, [2,3] and proteins embedded in them could carry out a wide range of physiological and biochemical processes. [1] Biological membranes supported on substrates are widely used to mimic the dynamics and structural features of cell membranes, [2,3] and proteins embedded in them could carry out a wide range of physiological and biochemical processes.…”