Cyclic peptides. VIII. Synthesis and tryptic hydrolysis of cyclic depsidipeptides containing a lysine residue.
Four stereoisomers of a cyclic depsidipeptide containing a lysine and a 2-hydroxy-3-phenylpropanoic acid (Hpp) residue have been synthesized and their susceptibility toward trypsin examined. Trypsin hydrolyzed cyclo(-L-Lys-L-Hpp-) (I-LL) and cyclo(-L-Lys-D-Hpp-) (I-LD) rapidly and cyclo(-D-Lys-L-Hpp-) (I-DL) and cyclo(-D-Lys-D-Hpp-) (I-DD) very slowly. Proteolytic coefficients of these substrates and a reference compound are shown as follows: I-LL, 112; I-LD, 34; I-DL, 0.34; I-DD, 0.11, and Ac-L-Lys-OEt, 44. Possible mode of actin of trypsin on these substrates was discussed.
D000595:Amino Acid Sequence; D006868:Hydrolysis; D007773:Lactates; D008239:Lysine; D010456:Peptides, Cyclic / Q000138:chemical synthesis*; D013237:Stereoisomerism; D014357:Trypsin
D007773:Lactates; D010456:Peptides, Cyclic; C017648:3-phenyllactic acid; D014357:Trypsin; D008239:Lysine