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Issue 4, 2012
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Self-assembly of human amylin-derived peptides studied by atomic force microscopy and single molecule force spectroscopy

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Abstract

The self-assembly of peptides and proteins into amyloid fibrils of nanometric thickness and up to several micrometres in length, a phenomenon widely observed in biological systems, has recently aroused a growing interest in nanotechnology and nanomedicine. Here we have applied atomic force microscopy and single molecule force spectroscopy to study the amyloidogenesis of a peptide derived from human amylin and of its reverse sequence. The spontaneous formation of protofibrils and their orientation along well-defined directions on graphite and DMSO-coated graphite substrates make the studied peptides interesting candidates for nanotechnological applications. The measured binding forces between peptides correlate with the number of hydrogen bonds between individual peptides inside the fibril structure according to molecular dynamics simulations.

Graphical abstract: Self-assembly of human amylin-derived peptides studied by atomic force microscopy and single molecule force spectroscopy

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Publication details

The article was received on 16 Sep 2011, accepted on 26 Oct 2011 and first published on 29 Nov 2011


Article type: Paper
DOI: 10.1039/C1SM06764H
Soft Matter, 2012,8, 1234-1242

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    Self-assembly of human amylin-derived peptides studied by atomic force microscopy and single molecule force spectroscopy

    J. J. Valle-Delgado, I. Liepina, D. Lapidus, R. Sabaté, S. Ventura, J. Samitier and X. Fernàndez-Busquets, Soft Matter, 2012, 8, 1234
    DOI: 10.1039/C1SM06764H

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