Τίτλος:
Self-assembly of a model amphiphilic oligopeptide incorporating an arginine headgroup
Γλώσσες Τεκμηρίου:
Αγγλικά
Περίληψη:
The self-assembly in aqueous solution of the alanine-rich peptide A 12R2 containing twelve alanine residues and two arginine residues has been investigated. This oligomeric peptide was synthesized via NCA-polymerization methods. The surfactant-like peptide is found via FTIR to form antiparallel dimers which aggregate into twisted fibrils, as revealed by cryogenic-transmission electron microscopy. The fibril substructure is probed via detailed X-ray scattering experiments, and are uniquely comprised of twisted tapes only 5 nm wide, set by the width of the antiparallel A12R 2 dimers. The packing of the alanine residues leads to distinct "β-sheet" spacings compared to those for amyloid-forming peptides. For this peptide, β-sheet structure coexists with some α-helical content. These ultrafine amyloid fibrils present arginine at high density on their surfaces, and this may lead to applications in nanobiotechnology. © 2013 The Royal Society of Chemistry.
Συγγραφείς:
Ian W. Hamley
Ashkan Dehsorkhi
Valeria Castelletto
Jani Seitsonen
Janne Ruokolainen
Hermis Iatrou
Εκδότης:
Royal Society of Chemistry (RSC)
Λέξεις-κλειδιά:
Alanine residues; Alanine-rich peptides; Amyloid fibril; Arginine residue; Helical content; Sheet structure; Surfactant-like peptides; Twisted tapes, Arginine; Glycoproteins; Oligomers; Self assembly; Transmission electron microscopy, Peptides
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