Antibacterial halogenoacetyl derivatives of amino acids and simple peptides

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Abstract
The vital role of D-alanine and L-lysine in the peptidoglycan crosslinking process in the bacterial cell wall prompted preparation of various small peptides incorporating these amino acids. N-Iodoacetyl or -bromoacetyl derivatives of the peptides then were prepared in the hope that they would serve as active-site-directed irreversible inhibitors of cell wall transpeptidases. Certain of the halogenoacetyl dipeptide esters, but not the corresponding free acids, showed slight antistaphylococcal activity. Subsequent structural variation showed that inclusion of D-alanine or L-lysine was not necessary, since antibacterial activity was at least as good when the dipeptide unit was replaced by glycylglycine or by an .omega.-aminoalkanoic acid. The observed antibacterial activity was probably not due to specific inhibition of a cell wall transpeptidase.

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