Lucignano, Rosanna (2024) Protein aggregation mechanisms: from amyloid fibrils to the design of new bionanomaterials. [Tesi di dottorato]

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Tipologia del documento: Tesi di dottorato
Lingua: English
Titolo: Protein aggregation mechanisms: from amyloid fibrils to the design of new bionanomaterials
Autori:
Autore
Email
Lucignano, Rosanna
rosanna.lucignano@unina.it
Data: 11 Marzo 2024
Numero di pagine: 224
Istituzione: Università degli Studi di Napoli Federico II
Dipartimento: Scienze Chimiche
Dottorato: Scienze chimiche
Ciclo di dottorato: 36
Coordinatore del Corso di dottorato:
nome
email
Lombardi, Angelina
alombard@unina.it
Tutor:
nome
email
Picone, Delia
[non definito]
Data: 11 Marzo 2024
Numero di pagine: 224
Parole chiave: aggregation, fibrils, nanocages, proteins, nanomaterials, biotechnology, structural biology
Settori scientifico-disciplinari del MIUR: Area 03 - Scienze chimiche > CHIM/03 - Chimica generale e inorganica
Depositato il: 22 Mar 2024 17:31
Ultima modifica: 16 Mar 2026 10:36
URI: http://www.fedoa.unina.it/id/eprint/15444

Abstract

Protein self-assembly processes play an important role in some severe neurodegenerative disorders, such as Alzheimer and Parkinson diseases. At the same time, the capability of some globular proteins to form ordered aggregates can be exploited to obtain novel nanostructured materials. Protein nanomaterials offer economic and environmental sustainability, due to their easy production, the possibility to fine tune their properties by molecular design and the biocompatibility. Their supramolecular assemblies can be characterized by 1D (fibrillar systems), 2D (films or functionalized surfaces) and 3D (hydrogels or hierarchical structures) dimensionality, thus they are suitable for a plethora of technological applications. This project aims to increase the basic knowledge about the proteins self-assembly properties and their supramolecular structures and to the design and production of novel materials for applications in nanomedicine and nanotechnology.

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