Solid-phase synthesis of hydroxyethylamine angiotensin analogues
| Autor: | Rob Ronald, David H. Kinder, Shelley L. Chambers, Jodie M. Hanesworth, Joseph W. Harding |
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| Rok vydání: | 1997 |
| Předmět: |
Male
Physiology Stereochemistry Peptide Alkylation Kidney Biochemistry Aminopeptidases Binding Competitive Rats Sprague-Dawley Cellular and Molecular Neuroscience Sodium borohydride chemistry.chemical_compound Automation Structure-Activity Relationship Endocrinology Solid-phase synthesis Adrenal Glands Structure–activity relationship Peptide bond Animals Methionyl Aminopeptidases Amino Acids chemistry.chemical_classification Membranes Hydrocarbons Halogenated Angiotensin II Metabolism Ketones Amino acid Rats chemistry Cattle |
| Zdroj: | Peptides. 18(4) |
| ISSN: | 0196-9781 |
| Popis: | Three hydroxyethylamine analogues of angiotensins II, III, and IV were prepared by solid-phase methods. The resin-bound peptide was alkylated with the iodomethylketone derivative of the N-terminal amino acid, followed by reduction to the alcohol using sodium borohydride. The iodomethylketones can be made in good yields from commercially available N-protected amino acids. The compounds were evaluated for their ability to displace labeled angiotensins from bovine adrenal membranes, and their metabolic stability tested in kidney homogenates and aminopeptidase M preparations. The hydroxyethylamine amide bond replacement reduced the affinity of the analogues; however, they were substantially more stable to enzymatic degradation. |
| Databáze: | OpenAIRE |
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