biostudies-literatureJi WInnovation Research Community Science FundChinese Academy of SciencesEuropean Research CouncilNational Natural Science Foundation of China7181-7190https://www.ebi.ac.uk/biostudies/studies/S-EPMC7616928biostudies-literatureUnknown14(6)Conformational transition of proteins and peptides into highly stable, β-sheet-rich structures is observed in many amyloid-associated neurodegenerative disorders, yet the precise mechanism of amyloid formation at the molecular level remains poorly understood due to the complex molecular structures. Short peptides provide simplified models for studying the molecular basis of the assembly mechanism that governs β-sheet fibrillation processes underlying the formation and inhibition of amyloid-like structures. Herein, we report a supramolecular coassembly strategy for the inhibition and transformation of stable β-sheet-rich amyloid-derived dipeptide self-assemblies into adaptable secondary structural fibrillar assemblies by mixing with bipyridine derivatives. The interplay between the type andACS nanoCoassembly-Induced Transformation of Dipeptide Amyloid-Like Structures into Stimuli-Responsive Supramolecular Materials.PMC761692821802144QYZDB-SSW-JSC0342152230721802143694426217732482182100551861145304Yuan CBera SLi JMakam PJi WChakraborty PRencus-Lazar SGazit EYan XfalseCoassembly-Induced Transformation of Dipeptide Amyloid-Like Structures into Stimuli-Responsive Supramolecular Materials.Conformational transition of proteins and peptides into highly stable, β-sheet-rich structures is observed in many amyloid-associated neurodegenerative disorders, yet the precise mechanism of amyloid formation at the molecular level remains poorly understood due to the complex molecular structures. Short peptides provide simplified models for studying the molecular basis of the assembly mechanism that governs β-sheet fibrillation processes underlying the formation and inhibition of amyloid-like structures. Herein, we report a supramolecular coassembly strategy for the inhibition and transformation of stable β-sheet-rich amyloid-derived dipeptide self-assemblies into adaptable secondary structural fibrillar assemblies by mixing with bipyridine derivatives. The interplay between the type and2020-01-01T00:00:00Z2020 Jun2026-06-03T05:21:02.451Z2025-04-04T02:36:10.481ZS-EPMC76169283242748210.1021/acsnano.0c02138