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In order to use tetrapyrrolic macrocyclic species in medical applications, the interactions of bovine serum albumin (BSA) with tetrakis-para-carboxyphenyl-porphyrin (H₂T(p-COOH) PP or TCPP) and Chlorin e6 (Ce6), under different conditions, were investigated by fluorescence spectroscopy and UV–VIS absorption spectroscopy and contrasted with molecular docking study. The binding constant (K_b) values at three different temperatures were calculated using the modified Stern–Volmer equation. The enthalpy change (ΔH) and entropy change (ΔS) were determined based on the van’t Hoff equation. The results of fluorescence spectroscopy indicate that static quenching is the dominant process resulting from the BSA-TCPP complex formation. In the case of the BSA-Ce6 complex, static quenching was confirmed too. Thermodynamic analysis indicated that hydrogen bonds and van der …