Cyclic peptides as proteases: A reevaluation

Research output: Contribution to journalArticlepeer-review

37 Scopus citations


A recent report [Atassi, M. Z. and Manshouri, T.(1993) Proc. Natl. Acad. Sci. USA 90, 8282-8286] described the design and synthesis of two 29-amino acid cyclic peptides that were reported to hydrolyze both ester and amide bonds with chymotrypsin-like or trypsin-like specificity. We have synthesized the trypsin-mimic peptide (TrPepz) and detect no activity toward either ester or peptide substrates. The same result was independently obtained by Wells et al. [Wells, J. A., Fairbrother, W. J., Otlewski, J., Laskowski, M., Jr., and Burnier, J. (1994) Proc. Natl. Acad. Sci. USA 91, 4110-4114.] Additionally, we found that Atassi and Manshouri failed to obtain accurate kinetic constants for trypsin- and chymotrypsin-catalyzed ester hydrolysis because the high concentrations of trypsin and chymotrypsin that they report using would have prevented evaluation of initial rates. These findings are incompatible with the claims, reported by Atassi and Manshouri, that TrPepz has trypsin-like activity.

Original languageEnglish (US)
Pages (from-to)4106-4109
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number10
StatePublished - May 10 1994

ASJC Scopus subject areas

  • General


Dive into the research topics of 'Cyclic peptides as proteases: A reevaluation'. Together they form a unique fingerprint.

Cite this