Reactivity of consecutive basic amino acid residues in peptides.
Different tetrapeptides of general formula L-Ala-X-X-Gly, possessing a basic doublet in the second and third position (X = Arg or Lys), have been synthesized as free or N-acetylated molecules. The chemical reactivity of the arginine guanidino group and of the lysine epsilon-amino group were studied using respectively the Sakaguchi and the ortho-diacetylbenzene reactions, in the tetrapeptides as well as in related molecules. In both cases, the colour yield is markedly influenced by the length of the polypeptide chain and by the relative positions of the arginine and lysine residues, suggesting the occurrence of intramolecular bonds within the tetrapeptide molecule. Tryptic hydrolysis of the tetrapeptides was followed by evaluating the amino acids or peptides which appear to be specific for the different possible cleavages at the arginyl or at the lysyl bonds. The susceptibility to trypsin of the carboxylic group of the second basic amino acid decreases progressively in the order Lys-Arg greater than Arg-Arg much greater than Lys-Lys greater than Arg-Lys, which shows a fair correlation with the intra-cellular cleavage of the bonds observed during the processing of preproteins of of the precursors of several physiologically active peptides.
D000595:Amino Acid Sequence; D001120:Arginine; D004151:Dipeptides / Q000138:chemical synthesis; D008239:Lysine; D008954:Models, Biological; D008958:Models, Molecular; D009842:Oligopeptides / Q000138:chemical synthesis; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D004151:Dipeptides; D009842:Oligopeptides; D001120:Arginine; D008239:Lysine