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Vorgias, C.

Publications and source records attributed to Vorgias, C..

2 recordsLinked to original sources

Uniquome: Construction and Decoding of a Novel Proteomic Atlas that Contains New Peptide Entities

Cellular and molecular uniqueness has recently gained eminent importance, due to the large amount of data produced by "-omics" technologies. Herein, we have constructed and decoded the "Uniquome", by introduction of the new peptide entities: (a) "Core Unique Peptide" (CrUP), defined as the peptide whose sequence is accommodated, specifically and exclusively, only in one protein in a given proteome, and also bears the minimum length of amino acid sequence; (b) "Composite Unique Peptide" (CmUP), defined as the peptide composed by the linear unification of CrUPs, when two or more successive in order CrUPs overlap one another; (c) "Family Unique Peptide" (FUP), defined as the CrUPs that are common between all members of a given family, but unique only for the protein members of the particular family, and (d) "Universal Unique Peptides" (UUPs), which are the common CrUPs in a given protein across organisms, carrying the important ability to securely identify a protein independently of an organism. By these entities as tool-box, we have analyzed the human and model organisms, respective, proteomes. We demonstrate that these novel peptide entities play a crucial role for protein identification, protein-function prediction, cell physiology, tissue pathology, therapeutic oncology and translational medicine. Finally, we suggest that across species the conserved sequences are not DNA nucleotides but CrUPs entities. One-Sentence SummaryWe constructed and decoded the "Uniquome", by introducing the new peptide entities Core Unique Peptide, Composite Unique Peptide, Family Unique Peptide and Universal Unique Peptide

molecular biology↗

Discovery and characterization of novel inhibitors against ALS-related SOD1(A4V) aggregation through screening of a chemical library using Differerential Scanning Fluorimetry (DSF)

Cu/Zn Superoxide Dismutase 1 (SOD1) is a 32-kDa cytosolic dimeric metalloenzyme that neutralizes superoxide anions into harmless oxygen and hydrogen peroxide. Mutations in SOD1 are associated with ALS, a disease causing motor neuron atrophy and subsequent mortality. These mutations exert their harmful effects through a gain of function mechanism, rather than loss of function. Despite extensive research, the specific mechanism causing selective motor neuron death still remains unclear. A defining feature of ALS pathogenesis is protein misfolding and aggregation, evidenced by ubiquitinated protein inclusions containing SOD1 in motor neurons. This work aims to identify compounds countering SOD1(A4V) misfolding and aggregation, potentially aiding ALS treatment. The approach employed is drug repurposing and in vitro screening of a 1280 pharmacologically active compounds library, LOPAC(R). Using Differential Scanning Fluorimetry Technique (DSF), compounds were tested for their impact on SOD1(A4V) thermal stability. Screening revealed one compound raising protein-ligand Tm by 7{degrees}C, eight inducing a higher second Tm, suggesting stabilzation effect, and five reducing Tm up to 18{degrees}C, suggesting possible interactions or non-specific binding.

biochemistry↗