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Polar Interfacial Interactions in RPLC
Author(s) -
van Oss C.J.
Publication year - 1990
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.199000025
Subject(s) - chemistry , van der waals force , polar , hydrogen bond , electrokinetic phenomena , aqueous solution , hydrophobic effect , surface tension , chemical physics , ethylene glycol , chemical polarity , elution , particle (ecology) , chromatography , analytical chemistry (journal) , molecule , organic chemistry , thermodynamics , physics , oceanography , astronomy , geology
The three principal forces that govern the interaction between dissolved proteins and solid (flat or particulate) surfaces immersed in a polar liquid are: A. Lifshitz‐van der Waals forces (LW interactions) B. Polar (hydrogen bond, or Lewis acid‐base) forces (AB interactions, which include “hydrophobic” interactions) C. Electrostatic forces (EL interactions) EL interaction energies can be determined via electrokinetic measurements. LW and AB interaction energies are derived from the LW component and the electron‐acceptor (γ⊕) and electron‐donor (γ⊖) parameters of the AB component of the surface tension, all three of which can be determined by contact angle (Θ) measurements on (a) hydrated layers of protein and (b) flat layers of particulate surface, using at least 3 polar liquids in each case. By this approach, the optimal conditions for attachment as well as for detachment of a given protein to a well‐characterized solid surface or particle can be determined quantitatively. Reversed phase liquid chromatography of immunoglobulin G (1) on phenyl Sepharose (2) shows that the elution of the protein, by an increasing concentration of ethylene glycol (EG) in the aqueous medium (3), occurs at the EG concentration where the value of ΔG 132 TOT changes from negative to positive.