The nonapeptide YAGAVVNDL has previously been shown to specifically inhibit ribonucleotide reductase (RR) induced by herpes simplex virus (HSV) and other herpesviruses. The stability of this peptide has been examined in extracts of HSV-infected cells. It was found to be rapidly modified to yield free tyrosine and the octapeptide AGAWNDL. Modification could be inhibited by several protease inhibitors, suggesting that it arises through cleavage of the amino-terminal tyrosine peptide bond. The implications of these results for the development of a therapeutically useful drug based on the nonapeptide are discussed.
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