Hofmeister challenges: Ion binding and charge of the BSA protein as explicit examples

Luca Medda, Brajesh Barse, Francesca Cugia, Mathias Boström, Drew F. Parsons, Barry W. Ninham, Maura Monduzzi, Andrea Salis*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    81 Citations (Scopus)


    Experiments on bovine serum albumin (BSA) via potentiometric titration (PT) and electrophoretic light scattering (ELS) are used to study specific-ion binding. The effect is appreciable at a physiological concentration of 0.1 M. We found that anions bind to the protein surface at an acidic pH, where the protein carries a positive charge (Zp > 0), according to a Hofmeister series (Cl- < Br- < NO3 - < I- < SCN-), as well as at the isoionic point (Zp = 0). The results obtained require critical interpretation. The measurements performed depend on electrostatic theories that ignore the very specific effects they are supposed to reveal. Notwithstanding this difficulty, we can still infer that different 1:1 sodium salts affect the BSA surface charge/pH curve because anions bind to the BSA surface with an efficiency which follows a Hofmeister series.

    Original languageEnglish
    Pages (from-to)16355-16363
    Number of pages9
    Issue number47
    Publication statusPublished - 27 Nov 2012


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