Dipeptidyl-peptidase IV (DPP IV/CD26)-activated prodrugs: A successful strategy for improving water solubility and oral bioavailability

In the search of novel enzyme-based prodrug approaches to improve pharmacological properties of therapeutic drugs such as solubility and bioavailability, dipeptidyl-peptidase IV (DPP IV, also termed as CD26) enzyme activity provides a previously unexplored successful prodrug strategy. This review co...

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Detalles Bibliográficos
Autores: Velázquez, Sonsoles, Castro, Sonia de, Diez-Torrubia, Alberto, Balzarini, Jan, Camarasa Rius, María José
Tipo de recurso: artículo
Fecha de publicación:2015
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/117655
Acceso en línea:http://hdl.handle.net/10261/117655
Access Level:acceso abierto
Palabra clave:Stability
water solubility
peptides
oral bioavailability
hydroxy-containing drugs
Amine-containing drugs
CD26 prodrugs
dipeptidyl peptidase IV
Descripción
Sumario:In the search of novel enzyme-based prodrug approaches to improve pharmacological properties of therapeutic drugs such as solubility and bioavailability, dipeptidyl-peptidase IV (DPP IV, also termed as CD26) enzyme activity provides a previously unexplored successful prodrug strategy. This review covers key aspects of the enzyme useful for the design of CD26-directed prodrugs. The proof-of-concept of this prodrug technology is provided for amine-containing agents by directly linking appropriate di- (or oligo)peptide moieties to a free amino group of a non-peptidic drug through an amide bond which is specifically hydrolized by DPP IV/CD26. Special emphasis is also made in discussing the design and synthesis of more elaborated tripartite prodrug systems, for further extension of the strategy to hydroxy-containing drugs. The application of this technology to improve water solubility and oral bioavailability of prominent examples of antiviral nucleosides is highlighted.