Human serum albumin (HSA) is an important biopharmaceutical agent that has the capacity to carry diverse molecules and increase their circulation half-life time, but also to function as a disease biomarker.

Different chromatographic and non-conventional approaches for its purification were explored by Raquel dos Santos together with Carina Figueiredo, Aline Viecinski, Ana Pina, Arménio Barbosa and Cecília Roque and are now published in the Journal of Chromatography A.

(A) Location of HSA ligands, warfarine (magenta), A6 A5 ligand (blue) and sulfisoxazole (yellow), in its 3-dimentional structure. (B) Interaction details of warfarine and HSA from the complex crystallographic structure (PDB ID: 2BXD). Binding mode results for the docking of A6 A5 (C) and sulfisoxazole (D) in HSA crystallographic structure (PDB ID: 2BXD) (hydrogen bonds in dotted green lines, cation-π interactions in yellow triangles).

dos Santos, R, Figueiredo C, Viecinski AC, Pina AS, Barbosa AJM, Roque ACA. 2018. Designed affinity ligands to capture human serum albumin. Journal of Chromatography A.

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