Cargando…
Gene design, fusion technology and TEV cleavage conditions influence the purification of oxidized disulphide-rich venom peptides in Escherichia coli
BACKGROUND: Animal venoms are large, complex libraries of bioactive, disulphide-rich peptides. These peptides, and their novel biological activities, are of increasing pharmacological and therapeutic importance. However, recombinant expression of venom peptides in Escherichia coli remains difficult...
Autores principales: | Sequeira, Ana Filipa, Turchetto, Jeremy, Saez, Natalie J., Peysson, Fanny, Ramond, Laurie, Duhoo, Yoan, Blémont, Marilyne, Fernandes, Vânia O., Gama, Luís T., Ferreira, Luís M. A., Guerreiro, Catarina I. P. I., Gilles, Nicolas, Darbon, Hervé, Fontes, Carlos M. G. A., Vincentelli, Renaud |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5240416/ https://www.ncbi.nlm.nih.gov/pubmed/28093085 http://dx.doi.org/10.1186/s12934-016-0618-0 |
Ejemplares similares
-
High-throughput expression of animal venom toxins in Escherichia coli to generate a large library of oxidized disulphide-reticulated peptides for drug discovery
por: Turchetto, Jeremy, et al.
Publicado: (2017) -
High Throughput Quantitative Expression Screening and Purification Applied to Recombinant Disulfide-rich Venom Proteins Produced in E. coli
por: Saez, Natalie J., et al.
Publicado: (2014) -
Strategies for Heterologous Expression, Synthesis, and Purification of Animal Venom Toxins
por: Rivera-de-Torre, Esperanza, et al.
Publicado: (2022) -
Development of a gene synthesis platform for the efficient large scale production of small genes encoding animal toxins
por: Sequeira, Ana Filipa, et al.
Publicado: (2016) -
A fast and specific fluorescent probe for thioredoxin reductase that works via disulphide bond cleavage
por: Li, Xinming, et al.
Publicado: (2019)