Improved Identification Performance of Lysine Glycation PTM using PSI-BLAST

Protein is essential to the overall health of the human body which undergoes various enzymatic modifications referring as Post-translational modification (PTM) which forms a mature product of protein. Glycation is one of the 40 ptms that are discovered so far, a non-enzymatic covalent bond of sugar and protein or lipid. It is a bio-maker for renal failure, diabetes and implicated in other health issues as well, imprinting significant importance for its site identification in a protein sequence. Manual researches in the laboratory are quite expensive and prolonged. In modern times, computerized tools for ptm prediction is very popular and useful. In our experiment, we intended to improve Glycation prediction using an alternate feature extraction method, called Position-Specific Iterative Basic Local Alignment Search Tool (PSI-BLAST) deriving a position-specific scoring matrix (PSSM) and providing us 99% accuracy, 99.83% sensitivity, 99.15% specificity and 98.98% MCC by executing an Support vector machine (kernel=rbf) model outpacing the performance of an earlier developed tool GlyStruct.

[1]  A. Cornish-Bowden,et al.  IUPAC-IUB Joint Commission on Biochemical Nomenclature (JCBN). Nomenclature and symbolism for amino acids and peptides. Recommendations 1983. , 1984, European journal of biochemistry.

[2]  Karl W Barber,et al.  The ABCs of PTMs. , 2018, Nature chemical biology.

[3]  Yan Liu,et al.  Predict and Analyze Protein Glycation Sites with the mRMR and IFS Methods , 2015, BioMed research international.

[4]  Abdollah Dehzangi,et al.  GlyStruct: glycation prediction using structural properties of amino acid residues , 2019, BMC Bioinformatics.

[5]  Li Wang,et al.  Predicting lysine glycation sites using bi-profile bayes feature extraction , 2017, Comput. Biol. Chem..

[6]  James G. Lyons,et al.  SPIDER2: A Package to Predict Secondary Structure, Accessible Surface Area, and Main-Chain Torsional Angles by Deep Neural Networks. , 2017, Methods in molecular biology.

[7]  C. Calvo,et al.  Non enzymatic glycation of apolipoprotein A-I. Effects on its self-association and lipid binding properties. , 1988, Biochemical and biophysical research communications.

[8]  Pedro Domingues,et al.  Glycation and oxidation of histones H2B and H1: in vitro study and characterization by mass spectrometry , 2011, Analytical and bioanalytical chemistry.

[9]  Yu Xue,et al.  CPLM: a database of protein lysine modifications , 2013, Nucleic Acids Res..

[10]  F. Zhou,et al.  Gly-PseAAC: Identifying protein lysine glycation through sequences. , 2017, Gene.

[11]  S. Brunak,et al.  Analysis and prediction of mammalian protein glycation. , 2006, Glycobiology.

[12]  O. Jensen Modification-specific proteomics: characterization of post-translational modifications by mass spectrometry. , 2004, Current opinion in chemical biology.

[13]  Thomas L. Madden,et al.  Improving the accuracy of PSI-BLAST protein database searches with composition-based statistics and other refinements. , 2001, Nucleic acids research.

[14]  Jiangyan Dai,et al.  Glypre: In Silico Prediction of Protein Glycation Sites by Fusing Multiple Features and Support Vector Machine , 2017, Molecules.