Significance of K(L/V)WX(I/L/V)P Epitope of the B2Gpi in Its (Patho)Physiologic Function

β2-glycoprotein I (β2GPI) is a major autoantigen of autoimmune thrombophilia, known as the antiphospholipid syndrome. The exact mechanism underlying the β2GPI's involvement in the disease is not fully elucidated, as it is not its physiological role. We used random phage peptide library to identify sequences binding to β2GPI. Obtained K(L/V)WX(I/L/V)P motif, primarily designated as target unrelated, was confirmed as the selective binder of β2GPI. Based on this motif we confirmed the previously suggested role of polar residues in β2GPI interactions, and identified some already known and some new putative β2GPI binding proteins. The latter can help to further elucidate β2GPI's (patho)physiological role.