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Regioselective O-Glycosylation of Nucleosides via the Temporary 2',3'-Diol Protection by a Boronic Ester for the Synthesis of Disaccharide Nucleosides
Published on: July 26, 2018
Iminoboronatos: una nueva estrategia para la modificación reversible de proteínas
Pedro M S D Cal1, João B Vicente, Elisabete Pires
1Research Institute for Medicines and Pharmaceutical Sciences (iMed.UL), Faculty of Pharmacy, University of Lisbon, Av. Prof. Gama Pinto, 1649-003 Lisbon, Portugal.
Journal of the American Chemical Society
|May 31, 2012
Resumen
Los investigadores desarrollaron un nuevo método para la modificación de proteínas utilizando iminoboronatos estables. Esta técnica permite la modificación reversible de la lisina y los grupos de aminas N-terminales en soluciones acuosas, ayudando a los estudios biológicos.
Área de la Ciencia:
- Biología Química Biología química.
- La bioquímica es la bioquímica.
- Química orgánica es la química orgánica.
Sus antecedentes:
- La modificación de proteínas es crucial para el estudio de los procesos biológicos.
- Los métodos existentes enfrentan limitaciones en contextos fisiológicos.
Objetivo del estudio:
- Introducir una nueva estrategia para la modificación del grupo amino de la proteína.
- Para permitir la funcionalización de proteínas estable y reversible en medios acuosos.
Principales métodos:
- Formación de iminoboronatos estables con lisina y aminas N-terminales.
- Teoría Funcional de Densidad Utilizada (DFT) para conocimientos mecanicistas.
- Reversibilidad demostrada con analíticos específicos.
Principales resultados:
- Se logró una modificación estable y completa de los grupos de aminas.
- Se ha demostrado la formación reversible de iminoboronato en soluciones acuosas.
- Los cálculos de DFT apoyaron la estabilidad de los iminoboronatos contra la hidrólisis.
Conclusiones:
- La estrategia de iminoboronato presentada ofrece una herramienta robusta para la modificación de proteínas.
- La reversibilidad proporciona un control dinámico para aplicaciones biológicas.
- Este método mejora el estudio y la modulación de los procesos biológicos.
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02:04Covalently Linked Protein Regulators
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These groups modify specific amino acids in a protein.
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01:26Protein Modifications in the RER
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Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
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01:02Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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02:26Conservation of Protein Domains Over Different Proteins
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A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
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03:08Hydroboration-Oxidation of Alkenes
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02:54Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...