A5015797004- Alzheimer's disease research and treatments
- Supramolecular Self-Assembly in Materials
- Proteins in Food Systems
- Protein Structure and Dynamics
- Advanced Glycation End Products research
- Protein purification and stability
- Glycosylation and Glycoproteins Research
- Amino Acid Enzymes and Metabolism
University of Warsaw
2019-2023
Conformational transitions involving aggregated proteins or peptides are of paramount biomedical and biotechnological importance. Here, we report an unusual freeze-induced structural reorganization within a β-sheet-rich ionic coaggregate poly(l-lysine), PLL, poly(l-glutamic acid), PLGA. Freezing aqueous suspensions the PLL–PLGA β-aggregate in presence low concentrations salt (NaBr) induces instantaneous β-sheet-to-disorder transition, as probed by infrared spectroscopy amide I′ band region....
Canonical amyloid fibrils are composed of covalently identical polypeptide chains. Here, we employ kinetic assays, atomic force microscopy, infrared spectroscopy, circular dichroism, and molecular dynamics simulations to study fibrillization patterns two chimeric peptides, ACC1–13E8 ACC1–13K8, in which a potent amyloidogenic stretch derived from the N-terminal segment insulin A-chain (ACC1–13) is coupled octaglutamate or octalysine segments, respectively. While large electric charges prevent...
Canonical amyloid fibrils are composed of covalently identical polypeptide chains. Here, we employ kinetic assays, atomic force microscopy (AFM), infrared spectroscopy, circular dichroism (CD), and molecular dynamics (MD) to study fibrillization patterns two chimeric peptides, ACC1-13E8 ACC1-13K8, in which potent amyloidogenic stretch derived from the N-terminal segment insulin A-chain (ACC1-13) is coupled octaglutamate or octalysine segments, respectively. While large electric charges on...