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Titolo:
BINDING OF CYCLIC AND LINEAR MSH CORE PEPTIDES TO THE MELANOCORTIN RECEPTOR SUBTYPES
Autore:
SCHIOTH HB; MUCENIECE R; LARSSON M; MUTULIS F; SZARDENINGS M; PRUSIS P; LINDEBERG G; WIKBERG JES;
Indirizzi:
UPPSALA UNIV,BIOMED CTR,DEPT PHARMACEUT PHARMACOL,BOX 591 S-75124 UPPSALA SWEDEN LATVIAN ACAD SCI,INST ORGAN SYNTH,PHARMACOL LAB LV-226006 RIGA LATVIA UPPSALA UNIV,DEPT MED & PHYSIOL CHEM S-75124 UPPSALA SWEDEN
Titolo Testata:
European journal of pharmacology
fascicolo: 2-3, volume: 319, anno: 1997,
pagine: 369 - 373
SICI:
0014-2999(1997)319:2-3<369:BOCALM>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
MOLECULAR-CLONING; ALPHA-MELANOTROPIN; BIOLOGICAL-ACTIVITY; HORMONE; ANALOGS; EXPRESSION; ALANINE;
Keywords:
MELANOCORTIN RECEPTOR SUBTYPE; MSH (MELANOCYTE-STIMULATING HORMONE); LIGAND BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
H.B. Schioth et al., "BINDING OF CYCLIC AND LINEAR MSH CORE PEPTIDES TO THE MELANOCORTIN RECEPTOR SUBTYPES", European journal of pharmacology, 319(2-3), 1997, pp. 369-373

Abstract

We report here the binding of 5-, 6- and 7-amino-acid-long linear andcyclic core peptides of MSH (melanocyte-stimulating hormone) to cellstransiently expressing the human melanocortin MC(1), MC(2), MC(3) andMC(4) receptors. The results show that, in contrast to the natural peptides, the core peptides did not differentiate between the melanocortin MC(3) and MC(4) receptors. All tested cyclic peptides had much lower affinities than their corresponding linear homologues. Interestingly, the relative loss of binding due to the cyclisation did not change as the ring size decreased. Therefore, decreasing the ring size does not seem to force the peptide into a more unfavourable conformation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 13/07/20 alle ore 19:59:39