Structural and immunologic characterization of bovine, horse, and rabbit serum albumins

Abstract

Serum albumin (SA) is the most abundant plasma protein in mammals. SA is a multifunctional protein with extraordinary ligand binding capacity, making it a transporter molecule for a diverse range of metabolites, drugs, nutrients, metals and other molecules. Due to its ligand binding properties, albumins have wide clinical, pharmaceutical, and biochemical applications. Albumins are also allergenic, and exhibit a high degree of cross-reactivity due to significant sequence and structure similarity of SAs from different organisms. Here we present crystal structures of albumins from cattle (BSA), horse (ESA) and rabbit (RSA) serums. The structural data are correlated with the results of immunological studies of SAs. We also analyze the conservation or divergence of structures and sequences of SAs in the context of their potential allergenicity and cross-reactivity. In addition, we identified a previously uncharacterized ligand binding site in the structure of RSA, and calcium binding sites in the structure of BSA, which is the first serum albumin structure to contain metal ions.

Adsorption of Bovine Serum Albumin on Carbon-Based Materials

“…Figure 4d is the crystal structure of Bovine Serum Albumin [36]. The experimental data was fitted using the pseudo-secondorder kinetic model.…”

“…Taking into account low porosity of the EGr materials with predominance of mesopores, alternative interpretations of the applicability of this equation, such as intra-particle diffusion controlled adsorption, are not likely to be relevant. Figure 4d is the crystal structure of Bovine Serum Albumin [36]. The experimental data was fitted using the pseudo-second-order kinetic model.…”

“…The helical content is 74% and each has seventeen conserved disulfide bonds and a free thiol group [36]. Protein Data Bank (PDB) number of the BSA used in our work was 3V03 [36].…”

“…The helical content is 74% and each has seventeen conserved disulfide bonds and a free thiol group [36]. Protein Data Bank (PDB) number of the BSA used in our work was 3V03 [36]. It is known that negatively charged groups of the first and second domains of the amino acid sequences of BSA (molecular mass 66.382 kDa and molecule dimensions 14 nm × 4 nm × 4 nm) [39] are positioned inside the globules, while the positively charged groups are located on the surface of the globule [40].…”

Using extensional flow to reveal diverse aggregation landscapes for three IgG1 molecules

“…The protein solution then enters the other syringe, ready to be shuttled back on the next pass. (b) Structures of BSA (PDB ID: 3V03) (Majorek et al, 2012), WFL and STT. The surface‐view scFv models of WFL and STT were built from the structure of their parent, MEDI_578 (PDB ID: 5jz7) (Dobson et al, 2016).…”