Multimerization Improves Targeting of Peptide Radio-Pharmaceuticals

Title:Multimerization Improves Targeting of Peptide Radio-Pharmaceuticals

Volume: 18 Issue: 17

Author(s): Giuseppe Carlucci, Hildo J.K. Ananias, Zilin Yu, Christophe Van de Wiele, Rudi A. Dierckx, Igle J. de Jong and Philip H. Elsinga

Affiliation:

Keywords: Multimerization, binding, avidity, cooperativity, valency, ligand design, nuclear imaging, nanotechnology

Abstract: Multimerization offers unique kinetic and thermodynamic properties to molecules. Multimeric ligands, characterized by multiple similar or different monomeric molecules tethered together, can bind several receptors simultaneously. Multimerization occurs also in nature. This process can be used to develop molecules with high diagnostic and therapeutic value. By altering parameters as linkers` length and flexibility, scaffold and backbones insertion, and ligands-receptors recognition, it is possible to provide high selectivity and binding affinity. The resultant multimeric ligand has a more favorable binding affinity than corresponding monomeric ligands.

Cite this article as:

Carlucci Giuseppe, J.K. Ananias Hildo, Yu Zilin, Van de Wiele Christophe, A. Dierckx Rudi, J. de Jong Igle and H. Elsinga Philip, Multimerization Improves Targeting of Peptide Radio-Pharmaceuticals, Current Pharmaceutical Design 2012; 18 (17) . https://dx.doi.org/10.2174/13816128112092501