Literature DB >> 1664421

Hydrolysis of oligoribonucleotides by alpha-helical basic peptides.

M Perello1, B Barbier, A Brack.   

Abstract

Poly(Leu-Lys-Lys-Leu) increases markedly the rate of hydrolysis of oligoribonucleotides. The polypeptide adopts and alpha-helical conformation in water in the presence of salt. Non-helical poly(Pro-Lys-Lys-Leu) is much less active. Ac-Leu-Lys-Lys-Leu-NHEt has no hydrolytic activity. Oligotetrapeptides Ac-(Leu-Lys-Lys-Leu)n-NHEt with increasing chain-length have been prepared by solid phase synthesis to evaluate the critical chain-length required for the hydrolytic activity. It is possible to correlate the activity to the propensity to form alpha-helices.

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Year:  1991        PMID: 1664421     DOI: 10.1111/j.1399-3011.1991.tb01423.x

Source DB:  PubMed          Journal:  Int J Pept Protein Res        ISSN: 0367-8377


  2 in total

1.  Design of peptide-acridine mimics of ribonuclease activity.

Authors:  C H Tung; Z Wei; M J Leibowitz; S Stein
Journal:  Proc Natl Acad Sci U S A       Date:  1992-08-01       Impact factor: 11.205

2.  Mutually stabilizing interactions between proto-peptides and RNA.

Authors:  Moran Frenkel-Pinter; Jay W Haynes; Ahmad M Mohyeldin; Martin C; Alyssa B Sargon; Anton S Petrov; Ramanarayanan Krishnamurthy; Nicholas V Hud; Loren Dean Williams; Luke J Leman
Journal:  Nat Commun       Date:  2020-06-19       Impact factor: 14.919

  2 in total

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