Charge effect on the colchicine binding-site of tubulin.
Poly(L-lysine) was found to enhance colchicine binding activity of brain tubulin to a several folds. Bases of biological interests that were tested and found to be inactive were spermine, spermidine and even L-lysine. Part of this enhance binding is due to the increase in the affinity of colchicine-tubulin interaction in the presence of poly(L-lysine). Moreover, poly(L-lysine) stabilized the colchicine binding site of tubulin against thermal denaturation.
D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D001923:Brain Chemistry; D003078:Colchicine / Q000378:metabolism*; D004563:Electrochemistry; D006041:Goats; D010455:Peptides / Q000494:pharmacology*; D011107:Polylysine / Q000494:pharmacology*; D011485:Protein Binding / Q000187:drug effects; D011489:Protein Denaturation; D014404:Tubulin / Q000378:metabolism*
D010455:Peptides; D014404:Tubulin; D011107:Polylysine; D003078:Colchicine