In antibody purification processes, affinity chromatography has been used with Staphylococcus aureus protein A (SpA) as the main ligand. In this work, we present a novel Staphylococcal Protein A (AviPure thereafter), a synthetic ligand analogue based on native SpA B domain, with a molecular weight of approximately 14 kDa. The binding affinity of mAbs to AviPure was evaluated using Surface Plasmon Resonance (SPR) and affinity chromatography methods. The equilibrium dissociation constant (K-D) between the AviPure and mAbs was systematically measured using 1:1 (Langmuir) model and found to be 4.7 x 10(-8) M, with constant of dissociation at k(d) <= 1.0 x 10(-3) s(-1) and k(a) being 3.1 x 10(4) M-1 s(-1). When immobilized on Sepharose, the AviPure ligand density was 429 nmol/g moist weight resin and was able to effectively bind immunoglobulin and Fc fragment samples with higher affinity and the most effective flow rate when using ligand - Sepharose beads was at 75 cm/h giving the dynamic binding capacity of 53 mg/mL and 91% recovery of IgG. Suitable ligands used in affinity purification should have a K-D <= 10(-6) M and a dissociation rate (k(a)) aver-aging 10(-3) M-1 s(-1) with the k d ranging between 10(3) - 10(8) M-1. Therefore, the AviPure ligand can be used as an alternative to the standard protein A ligand in the purification of mAbs and Fc-fused proteins.