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Enhanced solubility of proteins and peptides in nonpolar solvents through hydrophobic ion pairing
Author(s) -
Powers Michael E.,
Matsuura James,
Brassell James,
Manning Mark C.,
Shefter Eli
Publication year - 1993
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360330608
Subject(s) - chemistry , solubility , aqueous solution , solvent , denaturation (fissile materials) , octanol , sodium dodecyl sulfate , sodium , phase (matter) , inorganic chemistry , organic chemistry , chromatography , partition coefficient , nuclear chemistry
A new technique for enhancing the solubility of peptides and proteins in organic solvents is described. Complexation of polypeptides with stoichiometric amounts of an anionic detergent, such as sodium dodecyl sulfate (SDS), produces diminished aqueous solubility, but enhanced solubility in organic solvents. Consequently, the partitioning of a polypeptide into a nonpolar solvent can be increased by two to four orders of magnitude. In the case of an insulin–SDS complex, the solubility in 1‐octanol is more than tenfold greater than in water. In 1‐octanol, the native structure of insulin remains intact, as determined by CD spectroscopy, and the thermal denaturation temperature (T m ) is increased by approximately 50°C relative to unfolding in water. Finally, peptides and proteins can be extracted back into an aqueous phase provided the chloride concentration is sufficient to displace bound detergent molecules. © 1993 John Wiley & Sons, Inc.