Validation of l-Tellurienylalanine as a Phenylalanine Isostere.
Chembiochem
; 21(8): 1136-1139, 2020 04 17.
Article
em En
| MEDLINE
| ID: mdl-31742805
ABSTRACT
Mass cytometry (MC) and imaging mass cytometry (IMCTM ) have emerged as important tools for the study of biological heterogeneity. We recently demonstrated the use of l-2-tellurienylalanine (TePhe), a mimic of phenylalanine (Phe), as an MC- and IMC-compatible protein synthesis reporter. In this work, the biochemical similarity of TePhe and its cognate analogue, Phe, are examined in the context of the RNaseâ
S complex. Isothermal titration calorimetry studies show that incorporation of TePhe preserves the interaction of S-peptide with S-protein, and the dissociation constants for the interaction of the Phe and TePhe peptides are within a factor of two. The resulting RNaseâ
S complex is catalytically active without significant alterations in the enzyme's kinetic parameters. Furthermore, circular dichroism spectroscopy does not reveal any changes to the secondary structure of TePhe-substituted RNaseâ
S. These findings provide strong evidence that TePhe functions as a Phe isostere in the context of a folded protein. It is anticipated that incorporation of TePhe into peptides or peptidomimetic scaffolds will enable facile generation of MC and IMCTM probes.
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Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
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Fenilalanina
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Ribonuclease Pancreático
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Ribonucleases
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Telúrio
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article