Format

Send to

Choose Destination
J Med Chem. 1995 May 12;38(10):1820-5.

Inhibition of herpes simplex virus type 1 helicase-primase by (dichloroanilino)purines and -pyrimidines.

Author information

1
Department of Biochemistry, Stanford University Medical School, California 94305, USA.

Abstract

Herpes simplex virus type 1 (HSV1) encodes a heterotrimeric helicase-primase comprised of the products of three of the seven DNA replication-specific genes. Several dihalo-substituted derivatives of N2-phenylguanines and 2-anilinoadenines weakly inhibited the intrinsic DNA-dependent NTPase activity of the HSV1 helicase-primase, and these compounds inhibited the DNA-unwinding activity of the enzyme. The primase activity of the enzyme was strongly inhibited by 3,4- and 3,5-dichloroanilino derivatives of adenine and 2-aminopyrimidines. These compounds and nucleoside analogs of 2-(3,5-dichloroanilino)purines inhibited viral DNA synthesis in HSV1-infected HeLa cells in culture but also inhibited cellular DNA synthesis, likely as a result of inhibition of cellular primase and/or DNA polymerases.

PMID:
7752206
DOI:
10.1021/jm00010a027
[Indexed for MEDLINE]

Supplemental Content

Loading ...
Support Center