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Fine‐tuned broad binding capability of human lipocalin‐type prostaglandin D synthase for various small lipophilic ligands
Author(s) -
Kume Satoshi,
Lee Young-Ho,
Nakatsuji Masatoshi,
Teraoka Yoshiaki,
Yamaguchi Keisuke,
Goto Yuji,
Inui Takashi
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.02.001
Subject(s) - isothermal titration calorimetry , chemistry , hydrophobic effect , enthalpy , hydrogen bond , atp synthase , gibbs free energy , lipocalin , crystallography , stereochemistry , thermodynamics , enzyme , organic chemistry , molecule , biochemistry , physics
The hydrophobic cavity of lipocalin‐type prostaglandin D synthase (L‐PGDS) has been suggested to accommodate various lipophilic ligands through hydrophobic effects, but its energetic origin remains unknown. We characterized 18 buffer‐independent binding systems between human L‐PGDS and lipophilic ligands using isothermal titration calorimetry. Although the classical hydrophobic effect was mostly detected, all complex formations were driven by favorable enthalpic gains. Gibbs energy changes strongly correlated with the number of hydrogen bond acceptors of ligand. Thus, the broad binding capability of L‐PGDS for ligands should be viewed as hydrophilic interactions delicately tuned by enthalpy–entropy compensation using combined effects of hydrophilic and hydrophobic interactions.