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Titolo:
Production of cyclic peptides and proteins in vivo
Autore:
Scott, CP; Abel-Santos, E; Wall, M; Wahnon, DC; Benkovic, SJ;
Indirizzi:
Penn State Univ, Dept Chem, University Pk, PA 16802 USA Penn State Univ University Pk PA USA 16802 m, University Pk, PA 16802 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 24, volume: 96, anno: 1999,
pagine: 13638 - 13643
SICI:
0027-8424(19991123)96:24<13638:POCPAP>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
PERMUTED DIHYDROFOLATE-REDUCTASE; ESCHERICHIA-COLI; COMBINATORIAL TECHNOLOGIES; TYROSINASE GENE; DRUG DISCOVERY; LIBRARIES; SEQUENCES; APTAMERS; PATHWAY; SYSTEM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Benkovic, SJ Penn State Univ, Dept Chem, University Pk, PA 16802 USA Penn State Univ University Pk PA USA 16802 Pk, PA 16802 USA
Citazione:
C.P. Scott et al., "Production of cyclic peptides and proteins in vivo", P NAS US, 96(24), 1999, pp. 13638-13643

Abstract

Combinatorial libraries of synthetic and natural products are an importantsource of molecular information for the interrogation of biological targets. Methods for the intracellular production of libraries of small, stable molecules would be a valuable addition to existing library technologies by combining the discovery potential inherent in small molecules with the largelibrary sizes that can be realized by intracellular methods. We have explored the use of split inteins (internal proteins) for the intracellular catalysis of peptide backbone cyclization as a method for generating proteins and small peptides that are stabilized against cellular catabolism. The DnaEsplit intein from Synechocystis sp. PCC6803 was used to cyclize the Escherichia coil enzyme dihydrofolate reductase and to produce the cyclic, eight-amino acid tyrosinase inhibitor pseudostellarin F in bacteria. Cyclic dihydrofolate reductase displayed improved in vitro thermostability, and pseudostellarin F production was readily apparent in vivo through its inhibition of melanin production catalyzed by recombinant Streptomyces antibioticus tyrosinase. The ability to generate and screen for backbone cyclic products invivo is an important milestone toward the goal of generating intracellularcyclic peptide and protein libraries.

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Documento generato il 20/09/20 alle ore 23:35:51