Surface-Templated Fibril Growth of Peptide Fragments from the Shaft Domain of the Adenovirus Fibre Protein

Title: Surface-Templated Fibril Growth of Peptide Fragments from the Shaft Domain of the Adenovirus Fibre Protein

Volume: 18 Issue: 3

Author(s): Victoria L. Sedman, Emmanouil Kasotakis, Xinyong Chen, Stephanie Allen, Clive J. Roberts, Anna Mitraki and Saul J.B. Tendler

Affiliation:

Keywords: Adenovirus, amyloid, atomic force microscope, self-assembly, substrate interactionsAdenovirus, amyloid, atomic force microscope, self-assembly, substrate interactions

Abstract: Here we present a study of five analogues of a fragment from the shaft domain of the adenovirus fibre protein that readily form fibrils under a range of conditions. Using atomic force microscopy the fibrillisation of these peptides at the liquid/solid interface utilizing ordered crystalline substrates has been investigated. Our results demonstrate that the assembly pathway at the liquid/solid interface enables only the formation of truncated fibrillar structures, which align along the substrates underlying atomic lattice during growth. Furthermore, that the concentration and volume of solution applied can be used to directly control the density of fibrillar coverage at the surface.

Cite this article as:

L. Sedman Victoria, Kasotakis Emmanouil, Chen Xinyong, Allen Stephanie, J. Roberts Clive, Mitraki Anna and J.B. Tendler Saul, Surface-Templated Fibril Growth of Peptide Fragments from the Shaft Domain of the Adenovirus Fibre Protein, Protein & Peptide Letters 2011; 18 (3) . https://dx.doi.org/10.2174/092986611794578323

DOI https://dx.doi.org/10.2174/092986611794578323	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305