Crystal Structure and Interaction With Bovine Serum Albumin of Rare Earth Complex [Nd(α-C10H7CH2COO)3(C12H8N2)

Abstract

The title complex [Nd(α-C10H7CH2COO)3(C12H8N2)]2 has been synthesized by the reaction of Nd(NO3)3 · 6H2O with α-naphthyl acetic acid (NAA) and 1,10-phenanthroline (phen). The title complex has an inversion center. The structure of title complex was characterized by the method of IR, elemental analysis, and X-ray single crystal diffraction. The results show that title complex crystallizes in a triclinic system, space group P-1 with cell parameters a=11.7670(10) Å, b=12.6937(13) Å, c = 16.190(19) Å, α = 91.118(2)°, β = 106.290(2)°, γ=115.993(3)°, V = 2058(2)Å3, Dc=1.420 Mg/m3, Z=1, μ=1.313mm − 1, F(000)=890. Each Nd(III) atom is bridged by four α-naphthyl acetate. The Nd(III) atom is nine-coordinated by seven oxygen atoms from five α-naphthyl acetate and two nitrogen atoms from one phen molecule. Hydrogen bonds and aromatic π … π stacking interactions assemble the title complex into a three-dimensional network. After studying the interaction of title complex with bovine serum albumin (BSA) through multi-spectroscopic methods, the binding constant K b, corresponding thermodynamic parameters ΔH, ΔS, and ΔG at different temperatures, were calculated according to the van't Hoff equation. We can find that hydrophobic interaction force plays a major role between the title complex and BSA. The effect of title complex on the conformation of BSA were also analyzed by using synchronous fluorescence and FT-IR spectroscopy.