Quantitative structure-activity relations by the MTD-method for binding of nonapeptides to the HLA-A2.1 molecule.
Binding of large series of nonapeptides to the HLA-A2.1 molecule was studied by a group of Sette in order to predict strongly binding peptides with possible therapeutic interest. Here we establish QSAR-s for these series. The MTD-method was used for steric requirements concerning amino acidic side chains as well as side chain hydrophobicities. Binding of these peptides to the HLA-A2.1 molecule is favored by a lipophylic character of side chains for the anchor position 2 and 9 and for positions 1,3 and 6 and by steric features that allow predictions for some modified amino acidic residues in these positions that should increase the peptide-HLA-molecule affinity.
Bologa
C
C
Department of Chemistry, University of Timişoara, Romania.
Drugărin
D
D
Simon
Z
Z
D000596:Amino Acids / Q000502:physiology; D000949:Histocompatibility Antigens Class II / Q000378:metabolism* / Q000502:physiology; D015394:Molecular Structure; D010455:Peptides / Q000378:metabolism* / Q000502:physiology; D011485:Protein Binding
D000596:Amino Acids; D000949:Histocompatibility Antigens Class II; D010455:Peptides