pH dependence of the relative hydrophobicity and lipophilicity of amino acids and peptides measured by aqueous two‐phase and octanol–buffer partitioning

Volume: 61, Issue: 2, Pages: 71 - 79
Published: Dec 5, 2008
Abstract
Partitioning of a series of free amino acids, their derivatives, and homo-oligopeptides in aqueous dextran-PEG two-phase systems and octanol buffer systems was examined at pH values from 2.0 up to 12.5. The pH-dependent partition behavior of free amino acids and peptides in the two-phase systems was compared with that of monofunctional drug-like compounds and found to be clearly different. The differences observed indicate that the information...
Paper Details
Title
pH dependence of the relative hydrophobicity and lipophilicity of amino acids and peptides measured by aqueous two‐phase and octanol–buffer partitioning
Published Date
Dec 5, 2008
Volume
61
Issue
2
Pages
71 - 79
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