[D-Ala2]-Deltorphin I peptoid and retropeptoid analogues: synthesis, biological activity and conformational investigations
| Autor: | Biondi, Laura, Giannini, E., Filira, Fernando, Gobbo, Marina, Marastoni, M., Negri, L., Rocchi, Raniero |
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| Rok vydání: | 2004 |
| Předmět: |
conformation
Male Narcotics Synthetic derivatives Stereochemistry Deltorphin I Guinea Pigs Myenteric Plexus Peptide biological activity In Vitro Techniques Biochemistry chemistry.chemical_compound Mice Peptoids Vas Deferens Structural Biology Drug Discovery peptide synthesis polycyclic compounds Peptide synthesis Animals Muscle Skeletal Molecular Biology Pharmacology chemistry.chemical_classification opioid peptides Organic Chemistry beta-Cyclodextrins Peptoid Biological activity General Medicine retropeptoids Fluorescence Combinatorial chemistry deltorphin nervous system chemistry Amino Acid Substitution peptoids Deltorphin Molecular Medicine Oligopeptides |
| Zdroj: | Journal of peptide science info:cnr-pdr/source/autori:Laura Biondi; Elisa Giannini; Fernando Filira; Marina Gobbo; Lucia Negri; Raniero Rocchi/titolo:[D-Ala2]-Deltorphin I peptoid and retropeptoid analogues: synthesis, biological activity and conformational investigations./doi:10.1002%2Fpsc.566/rivista:Journal of peptide science (Print)/anno:2004/pagina_da:578/pagina_a:587/intervallo_pagine:578–587/volume:10 |
| ISSN: | 1075-2617 |
| DOI: | 10.1002/psc.566 |
| Popis: | The synthesis is described of a [D-Ala2]-deltorphin I peptoid analogue in which all amino acid residues have been substituted by the corresponding N-alkylglycine residues. The [D-Ala2]-deltorphin I retropeptoid was also prepared as well as [Ala1,D-Ala2]-deltorphin 1 and the corresponding peptoid. Structural investigations by FT-IR and fluorescence measurements were carried out on the synthetic analogues and on some [D-Ala2]-deltorphin 1 peptide–peptoid hybrids previously prepared. According to the fluorescence measurements the distance between the aromatic residues in the deltorphin I peptoid and retropeptoid is similar to that suggested for the δ- and µ-opioids, respectively. Measurements of CD in the presence of β-cyclodextrin, and some preliminary pharmacological experiments were also performed. No dichroic bands are present in the spectrum of the [Ntyr1,D-Ala2]-deltorphin I, but an increasing dichroic effect appears in the spectra of both the deltorphin I peptoid and retropeptoid. Activity tests on isolated organ preparations showed that the modifications made produced a dramatic decrease in the agonistic activity of the synthetic derivatives. Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd. |
| Databáze: | OpenAIRE |
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