http://www.cnr.it/ontology/cnr/individuo/prodotto/ID15272
Structural determinants of salmon calcitonin bioactivity: the role of the Leu-based amphipathic a-helix (Articolo in rivista)
- Type
- Label
- Structural determinants of salmon calcitonin bioactivity: the role of the Leu-based amphipathic a-helix (Articolo in rivista) (literal)
- Anno
- 2006-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1074/jbc.M603528200 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Andreotti G.; López Méndez B.; Amodeo P.; Castiglione Morelli M. A.; Nakamuta H.; Motta A.; (literal)
- Pagina inizio
- Pagina fine
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- Rivista
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
- Caratterizzazione dei dettagli strutturali che regolano l'attività della calcitonina, un ormone largamente utilizzato nella cura dell'osteoporosi e dell'ipercalcemia. Possibilità di progettare analoghi con attività farmacologica elevata ma senza effetti collaterali. (literal)
- Note
- Scopu (literal)
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Istituto di Chimica Biomolecolare del Consiglio Nazionale delle Ricerche, Comprensorio Olivetti, Edificio A, 80078 Pozzuoli (Napoli), Italy;
Dipartimento di Chimica, Università della Basilicata, 85100 Potenza, Italy;
Laboratory of Pharmacology, Department of Pharmaceutical Sciences, Faculty of Pharmaceutical Sciences, Hiroshima International University, Hirokoshingai 5-1-1, Kure, Hiroshima 737-0112, Japan. (literal)
- Titolo
- Structural determinants of salmon calcitonin bioactivity: the role of the Leu-based amphipathic a-helix (literal)
- Abstract
- Salmon calcitonin (sCT) forms an amphipathic helix in the region
9-19, with the C-terminal decapeptide interacting with the helix
(Amodeo, P., Motta, A., Strazzullo, G., Castiglione Morelli, M. A.
(1999) J. Biomol. NMR 13, 161-174). To uncover the structural
requirementsforthehormonebioactivity,weinvestigatedseveralsCT
analogs. They were designed so as to alter the length of the central
helixbyremovaland/orreplacementofflankingresiduesandbyselectively
mutating or deleting residues inside the helix.Thehelix content
was assessed by circular dichroism and NMR spectroscopies; the
receptor binding affinity in human breast cancer cell line T 47D and
the in vivo hypocalcemic activity were also evaluated. In particular, by
NMR spectroscopy and molecular dynamics calculations we studied
Leu23,Ala24-sCT in which Pro23 and Arg24 were replaced by helix
inducing residues. Compared with sCT, it assumes a longer
amphipathic?-helix, with decreased binding affinity and one-fifth of
the hypocalcemic activity, therefore supporting the idea of a relationship
between a definite helix length and bioactivity. From the analysis
of other sCT mutants, we inferred that the correct helix length is
located in the 9-19 region and requires long range interactions and
the presence of specific regions of residues within the sequence for
high binding affinity and hypocalcemic activity. Taken together, the
structural and biological data identify well defined structural parameters
of the helix for sCT bioactivity. (literal)
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