New Insights into Protein Aggregation in Condensed and Amyloid States

Dear Colleagues,

Protein aggregation has two pathways: the condensation pathway and the amyloid aggregation pathway. Recently, protein condensates formed by LLPS (liquid–liquid phase separation) are being discovered anew. The dense bodies in the cytoplasm and nucleus are formed mostly from intrinsically disordered proteins, which interact with RNAs, but they can also form from globular proteins. The condensates (membrane-less organelles) serve functional roles in cell storage and regulation. Another pathway of protein aggregation ends in irreversible amyloid fibrils. The mature amyloid fibrils have very compact and regular structures. Due to their stability and special mechanical and electrical properties, they are used as scaffolding materials, both in cells and in biotechnology. The amyloid fibrils also exhibit special opto-physical properties from bioluminescence, enhanced absorption, enhanced fluorescence of bound dyes, interaction with laser light, and, interestingly, the laser (from visible to IR) induces degradation of amyloid fibers (J. Chem. Phys. (2015), DOI: 10.1063/1.4933207). Amyloid structures exert some functional roles in different organisms, but by the majority they are seen as cytotoxic and therefore sequestered.

We welcome papers exploring new insights into the special optical and physico-chemical properties or papers on the biological roles of protein oligomers, condensates, and amyloid. Also, papers on specific inhibitory compounds for the process of amyloid or condensate formation would be welcome. Bioinformatic or experimental studies of the interaction of the aggregates with lipid membranes and other proteins would be considered. Theoretical methods can include interactome analysis and signaling pathways affected by the aggregated proteins, as well as molecular dynamics calculations.

Prof. Dr. Eva Žerovnik
Guest Editor

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• proteinopathies
• protein aggregation
• physico-chemical and biological properties of amyloid fibrils and protein condensates
• signal and light transduction
• interaction with lipid membranes
• aggregating protein interactomes
• bioinformatics and machine learning
• molecular dynamics