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1.
Expert Rev Proteomics ; 12(2): 159-69, 2015 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-25711416

RESUMEN

IL-23 is an important therapeutic target for the treatment of inflammatory diseases. Adnectins are targeted protein therapeutics that are derived from domain III of human fibronectin and have a similar protein scaffold to antibodies. Adnectin 2 was found to bind to IL-23 and compete with the IL-23/IL-23R interaction, posing a potential protein therapeutic. Hydrogen/deuterium exchange mass spectrometry and computational methods were applied to probe the binding interactions between IL-23 and Adnectin 2 and to determine the correlation between the two orthogonal methods. This review summarizes the current structural knowledge about IL-23 and focuses on the applicability of hydrogen/deuterium exchange mass spectrometry to investigate the higher order structure of proteins, which plays an important role in the discovery of new and improved biotherapeutics.


Asunto(s)
Terapia Biológica , Deuterio/química , Hidrógeno/química , Interleucina-23/química , Biología Computacional , Humanos , Interleucina-23/metabolismo , Espectrometría de Masas/métodos , Unión Proteica , Conformación Proteica , Receptores de Interleucina/química
2.
PLoS Genet ; 2(4): e57, 2006 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-16683034

RESUMEN

We report here on a chemical genetic screen designed to address the mechanism of action of a small molecule. Small molecules that were active in models of urinary incontinence were tested on the nematode Caenorhabditis elegans, and the resulting phenotypes were used as readouts in a genetic screen to identify possible molecular targets. The mutations giving resistance to compound were found to affect members of the RGS protein/G-protein complex. Studies in mammalian systems confirmed that the small molecules inhibit muscarinic G-protein coupled receptor (GPCR) signaling involving G-alphaq (G-protein alpha subunit). Our studies suggest that the small molecules act at the level of the RGS/G-alphaq signaling complex, and define new mutations in both RGS and G-alphaq, including a unique hypo-adapation allele of G-alphaq. These findings suggest that therapeutics targeted to downstream components of GPCR signaling may be effective for treatment of diseases involving inappropriate receptor activation.


Asunto(s)
Proteínas de Caenorhabditis elegans/genética , Caenorhabditis elegans/genética , Subunidades alfa de la Proteína de Unión al GTP/metabolismo , Proteínas RGS/metabolismo , Receptores Acoplados a Proteínas G/metabolismo , Triazoles/farmacología , Animales , Caenorhabditis elegans/efectos de los fármacos , Proteínas de Caenorhabditis elegans/metabolismo , Calcio/metabolismo , Línea Celular , Evaluación Preclínica de Medicamentos , Femenino , Subunidades alfa de la Proteína de Unión al GTP/genética , Humanos , Proteínas RGS/genética , Ensayo de Unión Radioligante , Ratas , Ratas Sprague-Dawley , Receptores Acoplados a Proteínas G/genética , Saccharomyces cerevisiae/genética , Proteínas de Saccharomyces cerevisiae/genética , Proteínas de Saccharomyces cerevisiae/metabolismo , Vejiga Urinaria/efectos de los fármacos , Vejiga Urinaria/metabolismo
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