Biotin-tagged probes for MMP expression and activation: design, synthesis, and binding properties.
The design and synthesis of biotin chain-terminated inhibitors (BTI) showing high affinity for matrix metalloproteinases (MMPs) on one side and high affinity for avidin through the biotinylated tag on the other are reported. The affinity of the designed BTI toward five different MMPs has been evaluated and the simultaneous formation of a highly stable ternary system Avidin-BTI-MMP clearly assessed. This system will permit the development of new approaches to detect, quantify, or collect MMPs in biological samples, with potential applications in vivo.
Dragoni
Elisa
E
Magnetic Resonance Center - University of Florence, Sesto Fiorentino, Italy.
Calderone
Vito
V
Fragai
Marco
M
Jaiswal
Rahul
R
Luchinat
Claudio
C
Nativi
Cristina
C
D001360:Avidin / Q000378:metabolism; D001710:Biotin / Q000378:metabolism*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D015195:Drug Design; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D015971:Gene Expression Regulation, Enzymologic; D045726:Metalloproteases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008958:Models, Molecular; D015335:Molecular Probes / Q000138:chemical synthesis* / Q000378:metabolism*; D011485:Protein Binding
D004791:Enzyme Inhibitors; D015335:Molecular Probes; D001360:Avidin; D001710:Biotin; D045726:Metalloproteases