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Pharmacological characterization of lipidized analogs of prolactin-releasing peptide with a modified C- terminal aromatic ring.
Prazienkova, V; Ticha, A; Blechova, M; Spolcova, A; Zelezna, B; Maletinska, L.
Afiliación
  • Prazienkova V; Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
  • Ticha A; Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
  • Blechova M; Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
  • Spolcova A; Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
  • Zelezna B; Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague, Czech Republic.
  • Maletinska L; Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague, Czech Republic. maletin@uochb.cas.cz.
J Physiol Pharmacol ; 67(1): 121-8, 2016 Feb.
Article en En | MEDLINE | ID: mdl-27010901
Prolactin-releasing peptide (PrRP) is an anorexigenic neuropeptide expressed in the brain where it regulates food intake and energy expenditure. The C-terminal Arg-Phe-NH2 of PrRP is crucial for its biological activity. In our previous study, we showed that PrRP analogs myristoylated or palmitoylated at the N- terminus seem to cross the blood-brain barrier and lower food intake following peripheral administration. In this study, myristoylated and palmitoylated PrRP31 analogs with a modified C-terminal Phe were designed and tested. Lipidized analogs containing Phe(31) replaced by aromatic non-coded amino acids or tyrosine revealed high binding affinity to rat pituitary RC-4B/C cells with endogenous PrRP and neuropeptide FF 2 receptors and to CHO-K1 cells overexpressing either PrRP or neuropeptide FF 2 receptors. The analogs also showed strong agonistic properties at the GPR10 receptor using the beta-lactamase reporter gene assay. Moreover, lipidized PrRP analogs, especially those that were palmitoylated, demonstrated strong and long-lasting anorexigenic effects in fasted mice after subcutaneous administration. The most efficient PrRP31 analogs with PheCl2(31), either palmitoylated or myristoylated at the N-terminus, are promising candidates for the study of food disorders, possibly for anti-obesity treatment. Despite the therapeutic potential in targeting central GPR10, the endogenous ligand PrRP cannot cross the blood-brain barrier. Understanding biological activity and transport of novel structural analogs of PrRP with a potential central anorexigenic effect is of key therapeutic significance.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Neuropéptidos / Hormona Liberadora de Prolactina Límite: Animals / Humans / Male Idioma: En Revista: J Physiol Pharmacol Asunto de la revista: FARMACOLOGIA / FISIOLOGIA Año: 2016 Tipo del documento: Article País de afiliación: República Checa Pais de publicación: Polonia
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Neuropéptidos / Hormona Liberadora de Prolactina Límite: Animals / Humans / Male Idioma: En Revista: J Physiol Pharmacol Asunto de la revista: FARMACOLOGIA / FISIOLOGIA Año: 2016 Tipo del documento: Article País de afiliación: República Checa Pais de publicación: Polonia