Designed peptides that assemble into cross-α amyloid-like structures
نویسندگان
چکیده
منابع مشابه
Amyloid-Like Structures Formed by Azobenzene Peptides: Light-Triggered Disassembly
Andreas A. Deeg,1 Tobias E. Schrader,2 Halina Strzalka,1, 3 Jose Pfizer,4 Luis Moroder,4 and Wolfgang Zinth1 1 Institute of BioMolecular Optics and Munich Center of Integrated Protein Science (CIPSM), Ludwig-Maximilians-University, 80538 Munich, Germany 2Jülich Centre for Neutron Science (JCNS), Forschungszentrum Jülich GmbH Outstation at FRM II, 85747 Garching, Germany 3Physical Chemistry Inst...
متن کاملDesigned α-sheet peptides inhibit amyloid formation by targeting toxic oligomers
Previous studies suggest that the toxic soluble-oligomeric form of different amyloid proteins share a common backbone conformation, but the amorphous nature of this oligomer prevents its structural characterization by experiment. Based on molecular dynamics simulations we proposed that toxic intermediates of different amyloid proteins adopt a common, nonstandard secondary structure, called α-sh...
متن کاملWhat drives amyloid molecules to assemble into oligomers and fibrils?
We develop a theory for three states of equilibrium of amyloid peptides: the monomer, oligomer, and fibril. We assume that the oligomeric state is a disordered micellelike collection of a few peptide chains held together loosely by hydrophobic interactions into a spherical hydrophobic core. We assume that fibrillar amyloid chains are aligned and further stabilized by steric zipper interactions-...
متن کاملGlobular Tetramers of β2-Microglobulin Assemble into Elaborate Amyloid Fibrils
Amyloid fibrils are ordered polymers in which constituent polypeptides adopt a non-native fold. Despite their importance in degenerative human diseases, the overall structure of amyloid fibrils remains unknown. High-resolution studies of model peptide assemblies have identified residues forming cross-beta-strands and have revealed some details of local beta-strand packing. However, little is kn...
متن کاملTriphenylalanine peptides self-assemble into nanospheres and nanorods that are different from the nanovesicles and nanotubes formed by diphenylalanine peptides.
Understanding the nature of the self-assembly of peptide nanostructures at the molecular level is critical for rational design of functional bio-nanomaterials. Recent experimental studies have shown that triphenylalanine(FFF)-based peptides can self-assemble into solid plate-like nanostructures and nanospheres, which are different from the hollow nanovesicles and nanotubes formed by diphenylala...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Nature Chemical Biology
سال: 2018
ISSN: 1552-4450,1552-4469
DOI: 10.1038/s41589-018-0105-5