Structural characterisation of amyloid-like fibrils formed by an amyloidogenic peptide segment of β-lactoglobulin
Vasantha Gowda, Michal Biler, Andrei Filippov, Malisa V. Mantonico, Eirini Ornithopoulou, Mathieu Linares, Oleg N. Antzutkin, Christofer Lendel
Abstract
N-labelled amino acid residues at selected positions. We can conclude that the peptides form parallel β-sheets, but the NMR data was inconclusive regarding inter-sheet packing. Molecular dynamics simulations confirm the stability of parallel β-sheets and suggest two preferred modes of packing. Comparison of molecular dynamics models with NMR data and calculated chemical shifts indicates that both packing models are possible.
Topics & Concepts
FibrilPeptideNanoscopic scaleMolecular dynamicsChemistryAmyloid fibrilSolid-state nuclear magnetic resonanceNanomaterialsProtein structureChemical shiftCrystallographyBeta sheetNanotechnologyMaterials scienceComputational chemistryAmyloid βBiochemistryNuclear magnetic resonancePhysical chemistryMedicinePhysicsPathologyDiseaseProteins in Food SystemsProtein Structure and DynamicsSupramolecular Self-Assembly in Materials