After phase separation in two phase finite systems of zwitterionic surfactants or proteins in water, the electrolyte concentration is different in the two layers. We present the results for two different systems: 1) aqueous dispersions of dioctanoyl-phosphatidylcholine1 and 2) aqueous dispersions of lysozyme In both cases the presence of electrolytes significantly alters the phase separation curves.1,2 The concentration of the anion in the two phases is asymmetric, and depends primarily on the polarizability and size of the anion. In the case of lysozyme, the ion distribution between the two phases is discussed in terms of the protein surface roughness and of the specific binding sites [figure 1]. The competition for protein sites seems to be driven by dispersion forces missing from conventional theories that are limited to electrostatic forces alone. 1. J. Phys. Chem. B 2007, 111, 589-597. 2. J. Phys. Chem. B 2009, 113, 8124-8127.

Asymmetric partitioning of anions at interfaces: a Hofmeister series study / P.Lo Nostro; N.Peruzzi; M.Severi; B.Ninham; P.Baglioni. - In: ABSTRACTS OF PAPERS - AMERICAN CHEMICAL SOCIETY. - ISSN 0065-7727. - STAMPA. - 239:(2010), pp. ---. ((Intervento presentato al convegno 239th A.C.S. National Meeting tenutosi a San Francisco, CA nel 19-26 marzo 2010.

Asymmetric partitioning of anions at interfaces: a Hofmeister series study

LO NOSTRO, PIERANDREA;PERUZZI, NICCOLO';SEVERI, MIRKO;BAGLIONI, PIERO
2010

Abstract

After phase separation in two phase finite systems of zwitterionic surfactants or proteins in water, the electrolyte concentration is different in the two layers. We present the results for two different systems: 1) aqueous dispersions of dioctanoyl-phosphatidylcholine1 and 2) aqueous dispersions of lysozyme In both cases the presence of electrolytes significantly alters the phase separation curves.1,2 The concentration of the anion in the two phases is asymmetric, and depends primarily on the polarizability and size of the anion. In the case of lysozyme, the ion distribution between the two phases is discussed in terms of the protein surface roughness and of the specific binding sites [figure 1]. The competition for protein sites seems to be driven by dispersion forces missing from conventional theories that are limited to electrostatic forces alone. 1. J. Phys. Chem. B 2007, 111, 589-597. 2. J. Phys. Chem. B 2009, 113, 8124-8127.
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
239th A.C.S. National Meeting
San Francisco, CA
19-26 marzo 2010
P.Lo Nostro; N.Peruzzi; M.Severi; B.Ninham; P.Baglioni
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2158/776464
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