Interaction of polymers with amyloidogenic peptides

Abstract

With this review, the aim was to gather recent representative publications which describe the interaction of polymers with amyloidogenic peptides/proteins. When functional, these take part in for instance bacterial adhesion and biofilm formation. However, several of the peptides/proteins have been identified in various diseases. One of the current approaches to discover a cure against these relies on therapeutics which either prevent or accelerate peptide/protein aggregation and/or clear readily formed aggregates. Owing to the common interest of scientists from all disciplines to identify a cure against the diseases of public health concern, there are overwhelming numbers of publications dealing with these two approaches. Since amyloid aggregation could be regarded as a nucleated polymerization, which is an established mechanism of polymer self-assembly, we recently tackled the issue of amyloid aggregation using the theories and methods established in polymer science. In this review, we hence focus on gathering relevant and recent publications which describe the role of polymers in modulating the aggregation of amyloidogenic peptides/proteins.

Escherichia coli Biofilm Formation, Motion and Protein Patterns on Hyaluronic Acid and Polydimethylsiloxane Depend on Surface Stiffness

“…It should be noted that proteins in the curli appendages were not identified in the proteomes. This may have resulted from a low production of curli by the bacteria but also from the low solubility of such amyloid fibers [ 67 ], which may have led to their removal during the sample preparation prior to the mass spectrometry analysis. Thus, the protein production is consistent with the initiation or formation of biofilms on both HA surfaces, but the surface stiffness of the HA-2kPa positively regulates the production of proteins that are favorable to adhesion compared to the HA-44Pa.…”

Chemical Perspective of the Mechanism of Action of Antiamyloidogenic Compounds Using a Minimalistic Peptide as a Reductionist Model

“…Since our group is interested in the self-assembly of single amino acids, peptides, oligonucleotides, , biopolymers, − and heterocyclic compounds, , we thus initiated the investigation of the interaction of those compounds reported in the literature for their antiamyloidogenic effect on the full-length Aβ42 with FF fibers.…”