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

Juan José Valle-Delgado, Inta Liepina, Dmitrijs Lapidus, Raimon Sabaté, Salvador Ventura, Josep Samitier, Xavier Fernàndez-Busquets

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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. © 2012 The Royal Society of Chemistry.
Original languageEnglish
Pages (from-to)1234-1242
JournalSoft Matter
Volume8
Issue number4
DOIs
Publication statusPublished - 28 Jan 2012

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    Valle-Delgado, J. J., Liepina, I., Lapidus, D., Sabaté, R., Ventura, S., Samitier, J., & Fernàndez-Busquets, X. (2012). Self-assembly of human amylin-derived peptides studied by atomic force microscopy and single molecule force spectroscopy. Soft Matter, 8(4), 1234-1242. https://doi.org/10.1039/c1sm06764h