AI Article Synopsis
- The study focused on transporting three synthetic endothiopeptides into E. coli K12 mutant strains and assessing their enzymatic degradation.
- These peptides (AlaPsi[CSNH]Ala, AlaPsi[CSNH]Leu, and AlaPsi[CSNH]Phe) were effectively taken up by the bacteria through permeases.
- The synthesized peptides showed greater resistance to enzymatic cleavage compared to natural peptides, suggesting their potential use as carriers for enzyme inhibitors.
Article Abstract
Transport of three synthesized endothiopeptides: AlaPsi[CSNH]Ala, AlaPsi[CSNH]Leu, and AlaPsi[CSNH]Phe, into Escherichia coli K12 mutant strains and enzymatic degradation studies were carried out. These compounds, well transported by permeases, but significantly more resistant to enzymatic cleavage than the corresponding natural peptides, seem to be useful as enzyme inhibitor carriers.
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| http://dx.doi.org/10.1111/j.1574-6968.2008.01242.x | DOI Listing |
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