Crosslinking, salt-induced aging, and secondary structure formation in Peptide-containing coacervates inspired by spider silk.

Spider silks are exceptional biomaterials: biocompatible, biodegradable, and with remarkable mechanical properties. Unfortunately, attempts to replicate them tend to fail due to the difficulty of synthesizing the proteins that constitute them, and to an incomplete understanding of their processing conditions. Here, we report a synthetic system inspired by spider silk, consisting of a synthetic polyelectrolyte with grafted oligoalanine chains.

Probing How Anti-huntingtin Antibodies Bind the Fibrillar Fuzzy Coat Using Solid-State NMR.

Antibodies are critical for the immune response and serve as important tools due to their ability to recognize specific amino acid sequences, or epitopes. Based on the latter, they are utilized as diagnostic tools in biological and biomedical research. Huntington's disease (HD) is a neurodegenerative condition caused by CAG repeat expansions in the huntingtin (HTT) gene and characterized by amyloid-like protein deposits in patients.

Inhibitor-based modulation of huntingtin aggregation mechanisms mitigates fibril-induced cellular stress.

Huntington's disease (HD) is a neurodegenerative disorder in which mutated fragments of the huntingtin protein (Htt) undergo misfolding and aggregation. Since aggregated proteins can cause cellular stress and cytotoxicity, there is an interest in the development of small molecule aggregation inhibitors as potential modulators of HD pathogenesis. Here, we study how a polyphenol modulates the aggregation mechanism of huntingtin exon 1 (HttEx1) even at sub-stoichiometric ratios.

Photocontrol of the β-Hairpin Polypeptide Structure through an Optimized Azobenzene-Based Amino Acid Analogue.

A family of neurodegenerative diseases, including Huntington's disease (HD) and spinocerebellar ataxias, are associated with an abnormal polyglutamine (polyQ) expansion in mutant proteins that become prone to form amyloid-like aggregates. Prior studies have suggested a key role for β-hairpin formation as a driver of nucleation and aggregation, but direct experimental studies have been challenging. Toward such research, we set out to enable spatiotemporal control over β-hairpin formation by the introduction of a photosensitive β-turn mimic in the polypeptide backbone, consisting of a newly designed azobenzene derivative.