Anno2010
AutoriManno M, Giacomazza D, Newman J, Martorana V, San Biagio PL
AbstractThe formation of insulin amyloid fibrils is important not only for the development of reliable drugs but also for modeling the basic properties of protein self-assembly. Fibrillation kinetics is typically characterized by an initial apparent lag phase related to the formation of oligomers, protofibrils, and aggregation nuclei. Afterwards, aggregation proceeds over a wide range of length scales via fibril elongation, thickening, and/or flocculation and eventual gelation. By light scattering and rheological techniques, we reveal the structural details hidden in the apparent lag phase and we show the unexpected appearance of noteworthy elastic properties concurrently with initial fibril nucleation and elongation preceding the formation of the larger structures and the gel network.
RivistaLangmuir
ISSN
Impact factor
Volume26
Pagina inizio1424
Pagina fine1426
Autori IBFPier Luigi SAN BIAGIO, Mauro MANNO, Vincenzo MARTORANA, Daniela GIACOMAZZA
Linee di Ricerca IBFMD.P01.002.001
Sedi IBFIBF.PA