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Interaction of propafenone enantiomers with human α 1 ‐acid glycoprotein
Author(s) -
Oravcová Jana,
Lindner Wolfgang,
Szalay Peter,
Boháčik Ľubor,
Trnovec Tomáš
Publication year - 1991
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.530030107
Subject(s) - chemistry , enantiomer , propafenone , stereoselectivity , stereochemistry , binding site , biochemistry , medicine , cardiology , catalysis , atrial fibrillation
The interaction of propafenone enantiomers with human α 1 ‐acid glycoprotein was studied using high‐performance liquid chromatography. Each of the two optical antipodes interacted with one class of high‐affinity binding sites characterized by K a(R) = (6.18 ± 0.93) × 10 5 M −1 , n (R) = 1.34 ± 0.09 for the (R)‐isomer and K a(S) = (8.93 ± 1.82) × 10 5 M −1 , n (S) = 0.99 ± 0.08 for the (S)‐isomer. Nonspecific binding to secondary low‐affinity high‐capacity binding site(s) was only slightly greater in the case of the (S)‐enantiomer ( n ′ k ′ (S) = (1.06 ± 0.09) × 10 4 M −1 ) compared to the (R)‐enantiomer ( n ′ k ′ (R) = (6.87 ± 0.72) × 10 3 M −1 ). It was concluded that both enantiomers interact with common single class of high‐affinity binding sites on AAG (along with nonspecific binding) exhibiting only slight stereoselectivity for propafenone.