Effect of chain length on critical micelle formation and protein binding of quaternary ammonium compounds

The micelle formation tendency (log 1/CMC)) of a series of alkyldimethylbenzylammonium compounds is shown to be linearly dependent on the alky chain length, indicating no curling of the side chain up to C19. Protein binding of these charged molecules on the primary binding site for sulfaethiodole is...

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Bibliographic Details
Published in:Journal of medicinal chemistry 1976-06, Vol.19 (6), p.849-850
Main Authors: Lien, Eric J, Perrin, John H
Format: Article
Language:English
Subjects:
Binding Sites
Chemical Phenomena
Chemistry, Physical
Colloids
Kinetics
Micelles
Protein Binding
Quaternary Ammonium Compounds - metabolism
Regression Analysis
Serum Albumin, Bovine - metabolism
Structure-Activity Relationship
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Summary:The micelle formation tendency (log 1/CMC)) of a series of alkyldimethylbenzylammonium compounds is shown to be linearly dependent on the alky chain length, indicating no curling of the side chain up to C19. Protein binding of these charged molecules on the primary binding site for sulfaethiodole is shown to be parabolically dependent on the chain length with an optimal chain length around C16.
ISSN:0022-2623
1520-4804
DOI:10.1021/jm00228a025