Affinity probes for the avermectin binding proteins.
The design and synthesis of a series of avermectin affinity probes used in the identification and purification of the avermectin binding proteins is described. These modified avermectins fall into two design classes: ligands to covalently modify specific avermectin binding proteins [an 125I-labeled aryl azide photoprobe (15) and a tritiated aziridine analog (6)] and ligands for affinity chromatography applications [three biotinylated compounds (10, 12, and 13) and one resin-bound derivative (9)]. The binding affinities of these compounds for the Caenorhabditis elegans avermectin binding protein is presented as well as their biological activities against C. elegans and Artemia salina.
Meinke
P T
PT
Department of Basic Medicinal Chemistry, Merck Research Laboratories, Rahway, New Jersey 07065-0900.
Rohrer
S P
SP
Hayes
E C
EC
Schaeffer
J M
JM
Fisher
M H
MH
Mrozik
H
H
D000345:Affinity Labels / Q000138:chemical synthesis* / Q000378:metabolism; D000818:Animals; D000871:Anthelmintics / Q000378:metabolism*; D001156:Artemia; D017173:Caenorhabditis elegans / Q000378:metabolism; D007559:Ivermectin / Q000031:analogs & derivatives* / Q000378:metabolism; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D011955:Receptors, Drug / Q000378:metabolism*
D000345:Affinity Labels; D000871:Anthelmintics; D008024:Ligands; D011955:Receptors, Drug; D007559:Ivermectin; C019264:avermectin