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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. Cyclic peptides. VIII. Synthesis and tryptic hydrolysis of cyclic depsidipeptides containing a lysine residue. Yasutake, A., Miyazaki, K., Aoyagi, H., Kato, T., Izumiya, N. Int. J. Pept. Protein Res. (1980) [Pubmed]
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