Bartlomiej Fedorczyk

TL;DR: For the first time, a highly SABRE-active pyridine-based biocompatible molecular framework is incorporated into synthetic oligopeptides and preserved, demonstrating the importance of such earmarking.

TL;DR: Kinetic experiments indicate that the fibrillation is significantly accelerated not only in the presence of homologous seeds but also upon cross-seeding, suggesting thereby a common self-assembly theme for (L-Glu)n chains of various lengths.

TL;DR: The current findings suggest that the side chain elongation of the Lys1 by branching it with additional homoarginine (Har) residue, to obtain Lys(Har)-Pro-Pro-Arg, allows more effective inhibition of VEGF165/NRP-1 interaction.

TL;DR: A structure–activity relationship study of the systematic optimization of amino acid residues in positions 1–3 in the above tetrapeptides gives an important insight into structural requirements for high inhibitory activity on VEGF165/NRP‐1 interaction.

TL;DR: It is shown that conversion of α-helical (Glu)200 into amyloid-like β-fibrils is dramatically accelerated in the presence of intrinsically disordered (GLU)5, highlighting chain-length polydispersity as a potent, although so-far unrecognized factor profoundly affecting the fibrillation propensity of homopolypeptides.