Conformational Requirements for Activity of Salmon Calcitonin*
- 1 September 1985
- journal article
- research article
- Published by The Endocrine Society in Endocrinology
- Vol. 117 (3), 801-805
- https://doi.org/10.1210/endo-117-3-801
Abstract
A series of deletion-substitution analogs of salmon calcitonin (SCT) have been prepared containing combinations of a glycine substitution in position 8 and deletions of serine-2 and tyrosine-22. Biological activity of the analogs with respect to native SCT were determined in the rat hypocalcemic assay and by studying stimulation of cAMP formation and competition for binding of 125I-labeled SCT in T47 D human breast cancer cells. Each of the analogs retained full potency, irrespective of the means of assessment. It is suggested that conservation of the .alpha.-helical region of SCT, along with the overall tertiary structure, are more important for peptide potency than chain length per se.This publication has 9 references indexed in Scilit:
- Presence of an amphipathic helical segment and its relationship to biological potency of calcitonin analogsInternational Journal of Peptide and Protein Research, 1985
- Amphipathic helix and its relationship to the interaction of calcitonin with phospholipidsBiochemistry, 1983
- Biological Activities and Receptor Interactions of des-Leu16Salmon and des-Phe16Human Calcitonin*Endocrinology, 1983
- des-Ser2Salmon Calcitonin: A Biologically Potent Synthetic Analog*Endocrinology, 1981
- CALCITONIN AND 1,25-DIHYDROXYVITAMIN D3 RECEPTORS IN HUMAN-BREAST CANCER CELL-LINES1980
- Predicted secondary structure of calcitonin in relation to the biological activityBiochemical and Biophysical Research Communications, 1979
- STEROID RECEPTOR ANALYSES OF 9 HUMAN BREAST-CANCER CELL LINES1978
- EFFECT OF GUANYL NUCLEOTIDES ON PARATHYROID HORMONE-RESPONSIVE ADENYLATE CYCLASE IN CHICK KIDNEYJournal of Endocrinology, 1976
- Use of Helical Wheels to Represent the Structures of Proteins and to Identify Segments with Helical PotentialBiophysical Journal, 1967