Stability of New Carbapenem DA-1131 to Renal Dipeptidase (Dehydropeptidase I)

Author:

Park Sung Wook1,We Jeoung Soon1,Kim Gye Won2,Choi Seong Hak2,Park Haeng Soon1

Affiliation:

1. Department of Pharmacy, College of Pharmacy, Chonnam National University, Kwangju

2. and Research Laboratory, Dong-A Pharmaceutical Co., Ltd., Yongin, Kyunggi-Do, Korea

Abstract

ABSTRACT The stability of DA-1131 to renal dipeptidase (RDPase) (EC 3.4.13.19) was compared with that of imipenem and meropenem by V max / K m ratios as an index of the enzyme's preference for substrates. Our results showed a decreasing order of imipenem (6.24), meropenem (2.41), and DA-1131 (1.39). The biochemical evaluation of DA-1131 as the least preferred substrate of RDPase suggests its potential use as a novel β-lactam antibiotic which may be usable without coadministration of RDPase inhibitors once its clinical suitability is proven.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Reference24 articles.

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4. Edwards, J. R., P. J. Turner, C. Wannop, E. S. Withnell, A. J. Grindey, and K. Nairn. 1989. In vitro antibacterial activity of SM-7338, a carbapenem antibiotic with stability to dehydropeptidase I. Antimicrob. Agents Chemother.33:215-222.

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