title: Amyloid gels: precocious appearance of elastic properties during the formation of an insulin fibrillar network.
abstract: The 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.
authors.affiliation: Institute of Biophysics at Palermo, Italian National Research Council, via Ugo La Malfa 153, I90146 Palermo, Italy. mauro.manno@pa.ibf.cnr.it
authors.forename: Mauro
authors.initials: M
authors.lastname: Manno
authors.forename: Daniela
authors.initials: D
authors.lastname: Giacomazza
authors.forename: Jay
authors.initials: J
authors.lastname: Newman
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Martorana
authors.forename: Pier Luigi
authors.initials: PL
authors.lastname: San Biagio
mesh_terms: D000085:Acetates / Q000737:chemistry; D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D004548:Elasticity; D005782:Gels; D007328:Insulin / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D011485:Protein Binding; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D012996:Solutions; D013696:Temperature
chemical_list: D000085:Acetates; D000682:Amyloid; D005782:Gels; D007328:Insulin; D012996:Solutions