Structural Rearrangement from Oligomer to Fibril Detected with FRET in a Designed Amphiphilic Peptide
Sign Up to like & getrecommendations! Published in 2017 at "ChemBioChem"
DOI: 10.1002/cbic.201600436
Abstract: β‐Sheet conformation is promoted in peptides with amphiphilic design, and stable β‐turn formation is favored with the unnatural amino acid d‐Pro followed by a flexible residue such as Gly. A 19‐residue peptide (B3) was synthesized… read more here.
Keywords: oligomer fibril; fibril detected; rearrangement oligomer; detected fret ... See more keywords
The interaction of Aβ42 peptide in monomer, oligomer or fibril forms with sphingomyelin/cholesterol/ganglioside bilayers.
Sign Up to like & getrecommendations! Published in 2020 at "International journal of biological macromolecules"
DOI: 10.1016/j.ijbiomac.2020.11.112
Abstract: Aβ42 peptide binds neuronal membranes and aggregates into plaques that are characteristic of Alzheimer's disease. Aβ42 peptide has been proposed to be generated in membrane (nano) domains in the liquid-ordered phase, ganglioside GM1 being a… read more here.
Keywords: peptide; oligomer fibril; ganglioside; monomer oligomer ... See more keywords