Hydrolysis of oligoribonucleotides by alpha-helical basic peptides.
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.
Perello
M
M
Centre for Molecular Biophysics, C.N.R.S., Orléans, France.
Barbier
B
B
Brack
A
A
D000136:Acid-Base Equilibrium; D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D006868:Hydrolysis; D008239:Lysine / Q000737:chemistry; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D009843:Oligoribonucleotides / Q000737:chemistry*; D010472:Perchlorates; D017670:Sodium Compounds
D009842:Oligopeptides; D009843:Oligoribonucleotides; D010472:Perchlorates; D017670:Sodium Compounds; C031068:sodium perchlorate; D008239:Lysine