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Linear scaffolds for multivalent targeting of melanocortin receptors.
Dehigaspitiya, Dilani Chathurika; Anglin, Bobbi L; Smith, Kara R; Weber, Craig S; Lynch, Ronald M; Mash, Eugene A.
Afiliación
  • Dehigaspitiya DC; Department of Chemistry and Biochemistry, University of Arizona, Tucson, Arizona 85721-0041, USA. emash@email.arizona.edu.
Org Biomol Chem ; 13(47): 11507-17, 2015 Dec 21.
Article en En | MEDLINE | ID: mdl-26461460
ABSTRACT
Molecules bearing one, two, three, or four copies of the tetrapeptide His-dPhe-Arg-Trp were attached to scaffolds based on ethylene glycol, glycerol, and d-mannitol by means of the copper-assisted azide-alkyne cyclization. The abilities of these compounds to block binding of a probe at the melanocortin 4 receptor were evaluated using a competitive binding assay. All of the multivalent molecules studied exhibited 30- to 40-fold higher apparent affinites when compared to a monovalent control. These results are consistent with divalent binding to receptor dimers. No evidence for tri- or tetravalent binding was obtained. Differences in the interligand spacing required for divalent binding, as opposed to tri- or tetravalent binding, may be responsible for these results.
Asunto(s)

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Oligopéptidos / Receptor de Melanocortina Tipo 4 Límite: Humans Idioma: En Revista: Org Biomol Chem Asunto de la revista: BIOQUIMICA / QUIMICA Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Oligopéptidos / Receptor de Melanocortina Tipo 4 Límite: Humans Idioma: En Revista: Org Biomol Chem Asunto de la revista: BIOQUIMICA / QUIMICA Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos