Mechanism of inhibition of herpes simplex virus (HSV) ribonucleotide reductase by a nonapeptide corresponding to the carboxyl terminus of its subunit 2: specific binding of a photoaffinity analog, [4'-azido-Phe6]HSV H2-(6-15), to subunit 1

Herpes simplex virus (HSV) ribonucleotide reductase activity is specifically inhibited by a synthetic peptide, Tyr-Ala-Gly-Val-Val-Asn-Asp-Leu (HSV H2-(7-15)), corresponding to the carboxyl terminus of its subunit 2 (H2). In order to elucidate the mechanism of action of the nonapeptide a photoreactive analog, (4'-azido-Phe super(6))HSV H2-(6-15), was synthesized. The photoaffinity probe inhibits HSV ribonucleotide reductase activity, and when radioiodinated, it specifically labeled three viral proteins of 144, 95, and 85 kDa. The authors demonstrated that the nonapeptide interacts with H1.