Improved proteolytic stability and potent activity against Leishmania infantum trypanothione reductase of α/β-peptide foldamers conjugated to cell-penetrating peptides
The analytical data and overall yields of final α,β,-peptides 5-20 (Table S1), HPLC, HRMS or MALDI-TOF-MS of α,β,-peptide foldamers analogues, and proteolysis stability data are also included. Supplementary data related to this article can be found at https://doi.org/10.1016/j.ejmech.2017.09.032....
| Autores: | , , , , , , , , , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión enviada para evaluación y publicación |
| Fecha de publicación: | 2017 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/156688 |
| Acceso en línea: | http://hdl.handle.net/10261/156688 |
| Access Level: | acceso abierto |
| Palabra clave: | α/β-peptides Foldamers Proteolysis Protein-protein interactions Trypanothione reductase Leishmania infantum |
| Sumario: | The analytical data and overall yields of final α,β,-peptides 5-20 (Table S1), HPLC, HRMS or MALDI-TOF-MS of α,β,-peptide foldamers analogues, and proteolysis stability data are also included. Supplementary data related to this article can be found at https://doi.org/10.1016/j.ejmech.2017.09.032. |
|---|