作者: Carlos Polanco , José Lino Samaniego , Vladimir N. Uversky , Jorge Alberto Castañón-González , Thomas Buhse
关键词: Membrane protein 、 Peptide sequence 、 Chemistry 、 Protein aggregation 、 Amino acid 、 Amyloid 、 Biochemistry 、 UniProt 、 Intrinsically disordered proteins 、 Globular protein
摘要: There is a natural protein form, insoluble and resistant to proteolysis, adopted by many proteins independently of their amino acid sequences via specific misfolding-aggregation process. This dynamic process occurs in parallel with or as an alternative physiologic folding, generating toxic aggregates that are deposited accumulated various organs tissues. These proteinaceous deposits typically represent bundles β-sheet-enriched fibrillar species known the amyloid fibrils responsible for serious pathological conditions, including but not limited neurodegenerative diseases, grouped under term amyloidoses. The might adopt this conformation some globular natively unfolded (or intrinsically disordered) proteins. Our work shows disordered ordered can be reliably identified, discriminated, differentiated analyzing polarity profiles generated using computational tool index method (Polanco & Samaniego, 2009; Polanco et al., 2012; 2013; 2013a; 2014; 2014a; 2014b; 2014c; 2014d). We also show expressed neurons from these two groups based on profiles, used identify associated efficiency proposed high (i.e. 70%) evidenced analysis peptides APD2 database (2012), AVPpred (2013), CPPsite set selective antibacterial del Rio al. (2001), sets folded Oldfield (2005), human revised neurons, non-human Uniprot (2014), amyloidogenic AmyPDB (2014).