Document Type
Article
Publication Date
2015
Keywords
Polarity index method, natively unfolded proteins, intrinsically disordered proteins, natively folded proteins, neurons, amyloidosis, amyloid, amyloidogenic protein
Digital Object Identifier (DOI)
https://doi.org/10.18388/abp.2014_755
Abstract
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 to physiologic folding, generating toxic protein aggregates that are deposited and accumulated in various organs and tissues. These proteinaceous deposits typically represent bundles of β-sheet-enriched fibrillar species known as the amyloid fibrils that are responsible for serious pathological conditions, including but not limited to neurodegenerative diseases, grouped under the term amyloidoses. The proteins that might adopt this fibrillar conformation are some globular proteins and natively unfolded (or intrinsically disordered) proteins. Our work shows that intrinsically disordered and intrinsically ordered proteins can be reliably identified, discriminated, and differentiated by analyzing their polarity profiles generated using a computational tool known as the polarity index method (Polanco & Samaniego, 2009; Polanco et al., 2012; 2013; 2013a; 2014; 2014a; 2014b; 2014c; 2014d). We also show that proteins expressed in neurons can be differentiated from proteins in these two groups based on their polarity profiles, and also that this computational tool can be used to identify proteins associated with amyloidoses. The efficiency of the proposed method is high (i.e. 70%) as evidenced by the analysis of peptides and proteins in the APD2 database (2012), AVPpred database (2013), and CPPsite database (2013), the set of selective antibacterial peptides from del Rio et al. (2001), the sets of natively unfolded and natively folded proteins from Oldfield et al. (2005), the set of human revised proteins expressed in neurons, and non-human revised proteins expressed in neurons, from the Uniprot database (2014), and also the set of amyloidogenic proteins from the AmyPDB database (2014).
Rights Information
This work is licensed under a Creative Commons Attribution-Share Alike 4.0 License.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Acta Biochimica Polonica, v. 62, issue 1, p. 41-55
Scholar Commons Citation
Polanco, Carlos; Samaniego, José Lino; Uversky, Vladimir N N.; Castañón-González, Jorge Alberto; Buhse, Thomas; Leopold-Sordo, Marili; Madero-Arteaga, Alejandro; Morales-Reyes, Alicia; Tavera-Sierra, Lourdes; González-Bernal, Jesus A.; and Arias-Estrada, Miguel, "Identification of Proteins Associated with Amyloidosis by Polarity Index Method." (2015). Molecular Medicine Faculty Publications. 386.
https://digitalcommons.usf.edu/mme_facpub/386
