Perello M, Barbier B, Brack A
Centre for Molecular Biophysics, C.N.R.S., Orléans, France.
Int J Pept Protein Res. 1991 Aug;38(2):154-60. doi: 10.1111/j.1399-3011.1991.tb01423.x.
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.