Effect on the Conformation of a Terminally Blocked, (E) β,γ-Unsaturated δ-Amino Acid Residue Induced by Carbon Methylation
| Autor: | David Zanuy, Claudio Toniolo, Giulia Marafon, Alessandro Moretto, Carlos Alemán, Marco Crisma |
|---|---|
| Přispěvatelé: | Universitat Politècnica de Catalunya. Departament d'Enginyeria Química, Universitat Politècnica de Catalunya. IMEM-BRT- Innovation in Materials and Molecular Engineering - Biomaterials for Regenerative Therapies |
| Rok vydání: | 2019 |
| Předmět: |
conformation
crystal structure Chemistry Stereochemistry Organic Chemistry Chemistry Organic Enginyeria química::Química orgànica [Àrees temàtiques de la UPC] Methylation delta-amino acids DFT calculations Conformational study Foldamer Peptidemimetic peptidomimetics beta-turn Foldamer Conformational study Peptidemimetic Amino acid residue Química orgànica |
| Zdroj: | UPCommons. Portal del coneixement obert de la UPC Universitat Politècnica de Catalunya (UPC) Journal of organic chemistry (Online) 85 (2020): 1513–1524. doi:10.1021/acs.joc.9b02544 info:cnr-pdr/source/autori:Giulia Marafon, Alessandro Moretto, David Zanuy, Carlos Alemán, Marco Crisma, Claudio Toniolo/titolo:Effect on the Conformation of a Terminally Blocked, (E) beta,gamma-Unsaturated delta-Amino Acid Residue Induced by Carbon Methylation/doi:10.1021%2Facs.joc.9b02544/rivista:Journal of organic chemistry (Online)/anno:2020/pagina_da:1513/pagina_a:1524/intervallo_pagine:1513–1524/volume:85 |
| ISSN: | 1520-6904 0022-3263 |
| DOI: | 10.1021/acs.joc.9b02544 |
| Popis: | Peptides are well-known to play a fundamental therapeutic role and to represent building blocks for numerous useful biomaterials. Stabilizing their active 3D-structure by appropriate modifications remains, however, a challenge. In this study, we have expanded the available literature information on the conformational propensities of a promising backbone change of a terminally blocked delta-amino acid residue, a dipeptide mimic, by replacing its central amide moiety with an (E) C(beta)=C(gamma) alkene unit. Specifically, we have examined by DFT calculations, X-ray diffraction in the crystalline state, and FT-IR absorption/NMR spectroscopies in solution the extended vs folded preferences of analogues of this prototype system either unmodified or possessing single or multiple methyl group substituents on each of its four -CH2-CH=CH-CH2- main-chain carbon atoms. The theoretical and experimental results obtained clearly point to the conclusion that increasing the number of adequately positioned methylations will enhance the preference of the original sequence to fold, thus opening interesting perspectives in the design of conformationally constrained peptidomimetics. |
| Databáze: | OpenAIRE |
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