SELF-ASSEMBLY OF PROTEIN NANOSTRUCTURES AND RELATIONSHIP WITH DEGENERATIVE DISEASES
Proteins represent one of the most important molecules in living matter, as they accomplish a wide range of biological functions and play a crucial role in the maintenance of life. Their correct biological activity depends on their self-assembly into well-defined highly ordered three dimensional structures, a process denote as protein folding. Despite the number of checkpoints that exist to ensure proper folding in the progression from gene to a correctly folded functional protein, alterations can emerge due to undesirable interactions during the folding process which may lead to protein aggregation. A particularly interesting case of protein aggregation occurring both in vivo and in vitro is the conversion of specific proteins from their soluble functional native form into very stable and highly ordered fibrillar structures, termed as amyloid fibrils, through an alternative hierarchical self-
assembly process. The presence of fibrils and fibril deposits have been largely associated to a series of human diseases including numerous neurodegenerative disorders such as Alzheimer’s, Parkinson’s, type II diabetes, Creutzfeldt-Jakob and bovine spongiform encephalopathy diseases (8-9). Nevertheless, amyloids are not unequivocally connected to toxicity and disease provided that different organisms use their exceptional physico-chemical properties for important physiological roles (the so-called functional amyloids). Examples of such functional amyloid include bacterial coatings, catalytic scaffolds, agents mediating epigenetic information storage and transfer, adhesives, and structures for the storage of peptide hormones. Furthermore, another important emerging current in the study of amyloid fibrils is their in vitro synthesis from nontoxic proteins and peptides to serve in a very broad spectrum of technology applications as in food, biomedical, nanotechnology, or biomaterials industries. In this manner, we are interested in understanding the mechanisms of amyloid fibril formation, and their related structural and physical properties through the use of model protein systems provided that the phenomenon of amyloid fibrillation appears to reflect certain generic “polymeric” features of proteins. This research hence would allow us in both helping with the management of amyloid degenerative-related diseases, that is, by improving strategies toward the prevention of fibrillation processes, as well as to create new nanomaterials for different prospective technological applications.