       Document 0327
 DOCN  M9610327
 TI    Synthesis of tight binding inhibitors and their action on the
       proprotein-processing enzyme furin.
 DT    9601
 AU    Angliker H; Friedrich Miescher-Institut, Basel, Switzerland.
 SO    J Med Chem. 1995 Sep 29;38(20):4014-8. Unique Identifier : AIDSLINE
       MED/96005100
 AB    Furin is a subtilisin-like eukaryotic serine endoprotease which
       processes proproteins to biologically active proteins and peptides.
       Also, the envelope proteins of viruses, such as influenza and HIV
       viruses, need to be processed by furin for infectivity. This enzyme has
       a consensus substrate specificity for Arg-Xxx-Lys/Arg-Arg at the
       cleavage site. Two kinds of transition state analog peptides were
       designed and tested in vitro with furin. The ketomethylene series, psi
       (COCH2), have Ki's in the submicromolar range; the aminomethyl
       aminomethyl ketone series, psi(COCH2NH), have Ki's in the nanomolar
       range. The best inhibitor is Dec-Arg-Val-Lys-Arg-CH2-Ala-Val-Gly-NH2
       (2c) with a Ki of 3.4 nM.
 DE    Amino Acid Sequence  Molecular Sequence Data  Serine Proteinase
       Inhibitors/*CHEMICAL SYNTHESIS/PHARMACOLOGY  Structure-Activity
       Relationship  Subtilisins/*ANTAGONISTS & INHIB  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).

