Prediction of intrinsically disordered regions in proteins using signal processing methods: application to heat-shock proteins

• Published in: Medical & biological engineering & computing Vol. 54; no. 12; pp. 1831 - 1844
• Main Authors: Vojisavljevic, Vuk, Pirogova, Elena
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer Berlin Heidelberg 01.12.2016; Springer Nature B.V
• Subjects: Algorithms; Amino Acid Sequence; Amino acids; Animals; Apoptosis; Binding Sites; Biological activity; Biomedical and Life Sciences; Biomedical Engineering and Bioengineering; Biomedicine; Cancer; Cancer therapies; Cell death; Computer Applications; Diabetes mellitus; Enzymes; Function analysis; Heat shock proteins; Heat-Shock Proteins - chemistry; Heat-Shock Proteins - metabolism; Human Physiology; Humans; Imaging; Immunotherapy; Intrinsically Disordered Proteins - chemistry; Intrinsically Disordered Proteins - metabolism; Medical services; Mice; Neural networks; Neurodegenerative diseases; Original Article; Predictions; Protein structure; Proteins; Radiology; Signal processing; Signal Processing, Computer-Assisted; Structure-function relationships; Studies; Intrinsic disorder; Signal processing; Active/binding site; Cancer; HSPs
• ISSN: 0140-0118; 1741-0444; 1741-0444
• DOI: 10.1007/s11517-016-1477-x

Heat-shock protein (HSP)-based immunotherapy is believed to be a promising area of development for cancer treatment as such therapy is characterized by a unique approach to every tumour. It was shown that by inhibition of HSPs it is possible to induce apoptotic cell death in cancer cells. Interestingly, there are a great number of disordered regions in proteins associated with cancer, cardiovascular and neurodegenerative diseases, signalling, and diabetes. HSPs and some specific enzymes were shown to have these disordered regions in their primary structures. The experimental studies of HSPs confirmed that their intrinsically disordered (ID) regions are of functional importance. These ID regions play crucial roles in regulating the specificity of interactions between dimer complexes and their interacting partners. Because HSPs are overexpressed in cancer, predicting the locations of ID regions and binding sites in these proteins will be important for developing novel cancer therapeutics. In our previous studies, signal processing methods have been successfully used for protein structure–function analysis (i.e. for determining functionally important amino acids and the locations of protein active sites). In this paper, we present and discuss a novel approach for predicting the locations of ID regions in the selected cancer-related HSPs.