Synthesis and biological properties of 4-norleucine-neuropeptide Y; secondary structure of neuropeptide Y
| Autor: | J. C. Dobbs, Josef E. Fischer, Michael S. Nussbaum, R.S. Rapaka, Ambikaipakan Balasubramaniam, L.A. Carreira, D.F. Rigel, V. Renugopalakrishnan |
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| Rok vydání: | 1989 |
| Předmět: |
Agonist
Circular dichroism Stereochemistry medicine.drug_class Protein Conformation Norleucine Molecular Sequence Data Biophysics Neuropeptide Blood Pressure Spectrum Analysis Raman Biochemistry chemistry.chemical_compound Solid-phase synthesis Structural Biology Heart Rate mental disorders medicine Animals Neuropeptide Y Amino Acid Sequence Molecular Biology Protein secondary structure Fourier Analysis Circular Dichroism Biological activity Neuropeptide Y receptor humanities Rats chemistry Vasoconstriction |
| Zdroj: | Biochimica et biophysica acta. 997(3) |
| ISSN: | 0006-3002 |
| Popis: | Neuropeptide Y (NPY) is a 36 amino acid peptide amide isolated from porcine brain. The NPY analog, 4-norleucine-NPY was synthesized by a solid-phase method and purified to homogeneity in 20% yield by reverse-phase chromatography. Investigation of the biological properties indicated that the analog is an agonist of NPY. Secondary structural analyses revealed that NPY and the analog exhibited predominantly alpha-helical and beta-sheet structures, respectively; however, experiments in trifluoroethanol indicated that the analog has the potential of assuming an alpha-helical structure. Based on circular dichroism (CD), Raman spectroscopy and Chou-Fasman analyses, a model has been proposed for the secondary structure of NPY. |
| Databáze: | OpenAIRE |
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