Functionalized Proline-Rich Peptides Bind the Bacterial Second Messenger c-di-GMP.
Angew Chem Int Ed Engl
; 57(26): 7729-7733, 2018 06 25.
Article
en En
| MEDLINE
| ID: mdl-29521445
ABSTRACT
c-di-GMP is an attractive target in the fight against bacterial infections since it is a near ubiquitous second messenger that regulates important cellular processes of pathogens, including biofilm formation and virulence. Screening of a combinatorial peptide library enabled the identification of the proline-rich tetrapeptide Gup-Gup-Nap-Arg, which binds c-di-GMP selectively over other nucleotides in water. Computational and CD spectroscopic studies provided a possible binding mode of the complex and enabled the design of a pentapeptide with even higher binding strength towards c-di-GMP. Biological studies showed that the tetrapeptide inhibits biofilm growth by the opportunistic pathogen P. aeruginosa.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Péptidos
/
Pseudomonas aeruginosa
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Prolina
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Sistemas de Mensajero Secundario
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GMP Cíclico
Idioma:
En
Revista:
Angew Chem Int Ed Engl
Año:
2018
Tipo del documento:
Article
País de afiliación:
Suiza