Affinity capillary electrophoresis to examine receptor-ligand interactions.
Afffinity capillary electrophoresis (ACE) is a new analytical technique that has been shown to be an efficient and accurate tool in studying biomolecular noncovalent interactions and determining binding and dissociation constants of formed complexes. ACE uses as its basis the change in migration time of a receptor upon binding to a ligand found in the electrophoresis buffer. Subsequent Scatchard analysis using noninteracting markers realizes a binding constant. Herein, ACE and three modifications in the technique, partial-filling ACE (PFACE), flow through PFACE (FTPFACE), and multiple-step ligand injection ACE (MSLIACE) are used to probe the binding of ristocetin A (Rist A) and vancomycin (Van) from Streptomyces orientalis to D-Ala-D-Ala terminus peptides and carbonic anhydrase B (CAB, E.C.4.2.1.1) to arylsulfonamides.
Azad
Maryam
M
Department of Chemistry and Biochemistry, California State University, Los Angeles, CA., USA.
Kaddis
John
J
Villareal
Valerie
V
Hernandez
Lili
L
Silverio
Catherine
C
Gomez
Frank A
FA
D000900:Anti-Bacterial Agents / Q000737:chemistry; D001667:Binding, Competitive / Q000502:physiology*; D024401:Carbonic Anhydrase I / Q000737:chemistry*; D019075:Electrophoresis, Capillary / Q000379:methods; D008024:Ligands; D012310:Ristocetin / Q000737:chemistry*; D013302:Streptomyces / Q000737:chemistry; D014640:Vancomycin / Q000737:chemistry*
D000900:Anti-Bacterial Agents; D008024:Ligands; D012310:Ristocetin; C016719:ristocetin A; D014640:Vancomycin; D024401:Carbonic Anhydrase I