Bovine Serum Albumin is major transport protein and is often used as a drug carrier in body organs. Knowl-edge of its binding with metallosurfactant can significantly influence the biodistribution of metallodrugs.Current work demonstrated a facile method to prepare four different double chained metallosurfactantscontaining Fe, Co, Ni and Cu as part of their counter ion. The as-synthesized metallosurfactants werecharacterized using FTIR, AAS, TGA and XRD in solid form. The aggregation of these metallosurfactantsin aqueous medium was investigated through conductivity, surface tension and SAXS. Further, we haveinvestigated their binding with BSA through different analytical methods The effect of concentration ofmetallosurfactants on the primary and secondary structure of BSA was further examined by SDS-PAGEand Circular dichroism, respetively. It is found that at premicellar concentration, the primary structureof BSA was not affected but the secondary structure i.e.α-helical structure of BSA was altered as shownby circular dichroism. Interestingly, post micellar concentration of metallosurfactants shows the pro-nounced effect on the primary and secondary structure of BSA. SAXS study also supports the fact ofunfolding of protein and its wrapping around the micelles. Zeta potential describes the electrical chargeand stability of the protein in the presence of different concentration of metallosurfactant. Along with,it was found that presence of protein delays the aggregation behavior of metallosurfactant, as a sign of binding of BSA with metallosurfactant.