Design and NMR studies of cyclic peptides targeting the N-terminal domain of the protein tyrosine phosphatase YopH. (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Design and NMR studies of cyclic peptides targeting the N-terminal domain of the protein tyrosine phosphatase YopH. (Articolo in rivista) (literal)

Anno

• 2011-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1111/j.1747-0285.2010.01058.x (literal)

Alternative label

• Marilisa Leone, Elisa Barile, Russell Dahl, Maurizio Pellecchia (2011)
  Design and NMR studies of cyclic peptides targeting the N-terminal domain of the protein tyrosine phosphatase YopH.
  in Chemical biology & drug design (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Marilisa Leone, Elisa Barile, Russell Dahl, Maurizio Pellecchia (literal)

Pagina inizio

• 12 (literal)

Pagina fine

• 19 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 77 (literal)

Rivista

• Chemical biology & drug design (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

• 8 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 1 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Burnham Institute for Medical Research, La Jolla, CA, USA (literal)

Titolo

• Design and NMR studies of cyclic peptides targeting the N-terminal domain of the protein tyrosine phosphatase YopH. (literal)

Abstract

• We report on the design and evaluation of novel cyclic peptides targeting the N-terminal domain of the protein tyrosine phosphatase YopH from Yersinia. Cyclic peptides have been designed based on a short sequence from the protein SKAP-HOM [DE(pY)DDPF (pY = phosphotyrosine)], and they all contain the motif DEZXDPfK (where Z is a phosphotyrosine or a non-hydrolyzable phosphotyrosine mimetic, X is an aspartic acid or a leucine and f is a d-phenylalanine). These peptides present a 'head to tail' architecture, enabling cyclization through formation of an amide bond in between the side chains of the first aspartic acid and the lysine residues. Chemical shift perturbation studies have been carried out to monitor the binding of these peptides to the N-terminal domain of YopH. Peptides containing a phosphotyrosine moiety exhibit binding affinities in the low micromolar range; substitution of the phosphotyrosine with one of its non-hydrolyzable derivatives dramatically reduces the binding affinities. These preliminary studies may pave the way for the discovery of more potent and selective peptide-based ligands of the YopH N-terminal domain which could be further investigated for their ability to inhibit Yersiniae infections. (literal)

Prodotto di

• Caratterizzazione strutturale di biomolecole di interesse terapeutico mediante metodologie computazionali (PM.P01.022.002) (Modulo)
• Institute of biostructure and bioimaging (IBB) (Istituto)
• Determinazione della struttura tridimensionale di biomolecole complesse con tecniche spettroscopiche e cristallografiche (PM.P01.022.001) (Modulo)

Autore CNR

• MARILISA LEONE (Persona)

Incoming links:

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Caratterizzazione strutturale di biomolecole di interesse terapeutico mediante metodologie computazionali (PM.P01.022.002) (Modulo)
• Determinazione della struttura tridimensionale di biomolecole complesse con tecniche spettroscopiche e cristallografiche (PM.P01.022.001) (Modulo)

Autore CNR di

• MARILISA LEONE (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Chemical biology & drug design (Rivista)