Predicting The Binding Peptide Of TAP Molecules By Independent Component Analysis Method

In the adaptive immune response,major histocompatibility complex(MHC)class I molecules are capable of presenting antigenic peptides,which mainly depends on the translocation of antigenic peptides from the cytosol to the endoplasmic reticulum(ER)by TAP molecules.TAP is a heterodimer of TAP1 and TAP2,with each subunit consisting of a hydrophobic transmembrane domain TMD and a cytoplasmic nucleotide-binding domain NBD,in which the core TMD contains a peptide binding site.The transportation of antigenic peptides by TAP molecules includes at least two steps: the initial binding of the peptide to TAP and the translocation of the peptide under ATP hydrolysis.Then,the compounds of MHC class I molecules binding to antigenic peptides are presented to the cell surface for CD8+ T cells specific recognition,thereby initiating the immune response.The establishment of quantitative structure-activity relationship model of interaction between TAP molecules and antigenic peptides by independent component analysis on the basis of negentropy maximization can reduce the correlation between sample data and maximize the statistical independence.The experimental samples of 613 nonapeptide data sets are extracted from the database,and these amino acids are encoded by 3z coding and 5z coding which represent the physicochemical properties of amino acids(hydrophobicity,spatial property and chargeability)and amino acid sparse coding.The calculation results show that the AUC value of the prediction model is 0.88,and the specificity of binding TAP molecules to antigenic peptides is mainly reflected in the position of P1,P2,P3 and P9,and the amino acids at the P7 position also have certain impacts.