Abstract
C(2)-Symmetric azobenzene-amino acid/peptide hybrids containing stable E-azo moiety have been synthesized. Upon irradiation with long wavelength UV, these compounds isomerized to the Z-form, whose thermal reisomerization to the E isomer slowed down considerably. These compounds exhibited in vitro moderate to strong inhibition of mammalian cellular protease Subtilisin Kexin Isozyme-1, also called Site 1 Protease, which plays vital roles in cholesterol synthesis, lipid metabolism, bone formation, and viral infections.
2010 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acids / chemistry
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Amino Acids / pharmacology*
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Animals
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Azo Compounds / chemistry
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Azo Compounds / pharmacology*
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Crystallography, X-Ray
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Dose-Response Relationship, Drug
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Enzyme Inhibitors / chemical synthesis
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / pharmacology*
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Humans
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Models, Molecular
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Molecular Structure
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Peptides / chemical synthesis
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Peptides / chemistry
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Peptides / pharmacology*
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Proprotein Convertases / antagonists & inhibitors*
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Serine Endopeptidases
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Stereoisomerism
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Structure-Activity Relationship
Substances
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Amino Acids
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Azo Compounds
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Enzyme Inhibitors
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Peptides
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Proprotein Convertases
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Serine Endopeptidases
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membrane-bound transcription factor peptidase, site 1
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azobenzene