Yang, HaiouGurgel, Patrick VWilliams, D KeithBobay, Benjamin GCavanagh, JohnMuddiman, David CCarbonell, Ruben G2023-09-012023-09-012010-050952-34991099-1352https://hdl.handle.net/10161/28894Affinity ligand HWRGWV has demonstrated the ability to isolate human immunoglobulin G (hIgG) from mammalian cell culture media. The ligand specifically binds hIgG through its Fc portion. This work shows that deglycosylation of hIgG has no influence on its binding to the HWRGWV ligand and the ligand does not compete with Protein A or Protein G in binding hIgG. It is suggested by the mass spectrometry (MS) data and docking simulation that HWRGWV binds to the pFc portion of hIgG and interacts with the amino acids in the loop Ser383-Asn389 (SNGQPEN) located in the C(H)3 domain. Subsequent modeling has suggested a possible three-dimensional minimized solution structure for the interaction of hIgG and the HWRGWV ligand. The results support the fact that a peptide as small as a hexamer can have specific interactions with large proteins such as hIgG.AnimalsHumansEndopeptidasesPepsin AOligopeptidesStaphylococcal Protein AImmunoglobulin GNerve Tissue ProteinsLigandsSequence AlignmentBinding SitesAmino Acid SequenceProtein Structure, TertiaryProtein BindingModels, MolecularMolecular Sequence DataImmunoglobulin Fc FragmentsJournal article2023-09-01