Fibrillar aggregation and/or misfolding of peptides and proteins has received increasing attention due to the involvement of these molecules in a variety of neurodegenerative diseases, such as Alzheimer's, Parkinson’s and prion diseases. The underlying assembly pathways are often nucleation driven, leading to complex fibrous assemblies. We have taken the challenge to interfere with such fibrillation pathways either via synthetic model systems, or by designing artificial hybrid-molecules, composed of amyloid- and polymer/oligomer segments. We here discuss both approaches in terms of synthetic analogues, steric shielding, protein assembly, as well as conformational analysis. Starting from model-polymer systems, containing artificial folding elements, prepared by RAFT-/ROP/ADMET-polymerization, polymers or oligomers are attached to specific positions of assembling proteins, such as amyloid-Abeta-40 and parathyroid-hormone, PTH. These hybrid-systems, also composed of temperature-sensitive polymers and assembling proteins allow to understand the proteins conformation, subsequently modulating its assembly, as shown for parathyroid-hormone PTH and amyloid-Abeta-40. Another approach uses artificial beta-turns, embedded into amyloid-A-beta-40 peptides. It is shown that both, the chemical nature as well as the positioning of artificial beta-turn mimetics strongly influences the subsequent fibrillation-behavior, often leading to the beta-crosssheet as the thermodynamically most favorable conformation.

Modulating fibrillar assembly processes of proteins and peptides by polymers and folding elements

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.