BOKU - Universität für Bodenkultur Wien - Forschungsinformationssystem

Logo BOKU-Forschungsportal

Gewählte Publikation:

Gößler-Schöfberger R, Hesser G, Reif MM, Friedmann J, Duscher B, Toca-Herrera JL, Oostenbrink C, Jilek A..
(2012): A stereochemical switch in the aDrs model system, a candidate for a functional amyloid.
Arch Biochem Biophys. 2012; 522(2):100-106 FullText FullText_BOKU

Amyloid fibrils are commonly observed to adopt multiple distinct morphologies, which eventually can have significantly different neurotoxicities, as e.g. demonstrated in case of the Alzheimer peptide. The architecture of amyloid deposits is apparently also determined by the stereochemistry of amino acids. Post-translational changes of the chirality of certain residues may thus be a factor in controlling the formation of functional or disease-related amyloids. Anionic dermaseptin (aDrs), an unusual peptide from the skin secretions of the frog Pachymedusa dacnicolor, assembles to amyloid-like fibrils in a pH-dependent manner, which could play a functional role in defense. aDrs can be enzymatically converted into the diastereomer [D-Leu2]-aDrs by an L/D-isomerase. EM and AFM on fibrils formed by these isomers have shown that their predominant morphology is controlled by the stereochemistry of residue 2, whereas kinetic and thermodynamic parameters of aggregation are barely affected. When fibrils were grown from preformed seeds, backbone stereochemistry rather than templating-effects apparently dominated the superstructural organization of the isomers. Interestingly, MD indicated small differences in the conformational propensities between the isomers. Our results demonstrate how D-amino acid substitutions could take active part in the formation of functional or disease-related amyloid. Moreover, these findings contribute to the development of amyloid-based nanomaterials. (C) 2012 Elsevier Inc. All rights reserved.
Autor*innen der BOKU Wien:
Oostenbrink Chris
Reif Maria
Toca-Herrera José Luis
BOKU Gendermonitor:

Find related publications in this database (using NML MeSH Indexing)
Amphibian Proteins - chemistry
Amyloid - chemistry
Antimicrobial Cationic Peptides - chemistry
Kinetics -
Microscopy, Atomic Force -
Microscopy, Electron, Transmission -
Models, Molecular -
Molecular Dynamics Simulation -
Spectroscopy, Fourier Transform Infrared -
Stereoisomerism -
Thermodynamics -

Find related publications in this database (Keywords)
D-Amino acid
Bioactive peptide
Functional amyloid
Posttranslational modification
Amphibian skin

© BOKU Wien Impressum