Abstract
Theophylline (Th) has been selectively conjugated to the four amino groups of melittin (Mel) by solid phase peptide synthesis. The cytolytic activity of the resultant Th-Mel compounds was tested on liposomes trapping the bovine serum albumin (BSA) conjugate with 4,7-bis(chlorosulfophenyl)-1,10-phenanthrol ine-2,9-dicarboxylic acid (BCPDA). The loss of lytic activity was the highest for Th-K7-Mel. Th-G1-Mel retains almost the same lytic activity as Mel. A homogeneous liposome time-resolved fluoroimmunoassay (LITRFIA) of Th in serum has been carried out with Th-G1-Mel between 5 ng and 10 microg.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Antibodies / immunology
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Calibration
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Dose-Response Relationship, Drug
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Europium
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Fluorescent Dyes / metabolism
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Fluoroimmunoassay / methods*
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Haptens / immunology
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Humans
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Liposomes / chemistry
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Liposomes / metabolism*
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Melitten / analogs & derivatives*
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Melitten / metabolism
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Melitten / pharmacology
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Molecular Sequence Data
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Permeability / drug effects
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Phenanthrolines / metabolism
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Sensitivity and Specificity
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Serum Albumin / metabolism
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Substrate Specificity
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Theophylline / analogs & derivatives*
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Theophylline / blood*
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Theophylline / immunology
Substances
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Antibodies
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Fluorescent Dyes
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Haptens
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Liposomes
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Phenanthrolines
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Serum Albumin
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4,7-bis(chlorosulfophenyl)-1,10-phenanthroline-2,9-dicarboxylic acid
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Melitten
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Europium
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Theophylline