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Possible participation of membrane thiol groups on the mechanism of NAD(P)+-stimulated Ca2+ efflux from mitochondria |
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| Authors: | A E Vercesi |
| Institution: | Department of Chemistry, University of Louisville, Louisville, Kentucky 40292 USA;Clinical Research Institute of Montreal Montreal, Quebec H2W 1R7 Canada;Chemical Institute Department of Organic Chemistry, University of Aarhus DK-8000 Aarhus C Denmark |
| Abstract: | The in vitro opioid activities of a series of leucine enkephalin analogs containing a thioamide linkage in place of the peptide bond at various positions of the backbone were determined in mu- and delta-receptor-selective bio- and binding-assays. Thioamide substitution in the 1-2 position resulted in an inactive compound, whereas the same modification in the 2-3 and 4-5 position produced potency enhancement. Most interestingly, the 2-3 modified analog showed a 3 to 5 times higher preference for delta- over mu-receptors than natural leucine enkephalin. These results suggest that subtle backbone modifications can have a profound effect on receptor affinity and selectivity of biologically active peptides. |
| Keywords: | EGTA ethylene glycol bis (β-aminoethyl ether) N N′-tetraacetic acid HEPES 4-(2-hydroxyethyl)-1-piperazineethane-sulfonic acid TMPD N N N′ N′-tetramethyl-p-phenylenediamine OAA oxaloacetate BOH β-hydroxybutyrate BA bongkrekate CAT carboxyatractyloside DIAMIDE diazenedicarboxylic acid bis-dimethylamide |
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