Structure-based design of a fluorimetric redox active peptide probe.
Structure-based iterative design was used to prepare a disulfide-containing nonapeptide as a fluorimetric probe for chemical and biochemical disulfide forming and breaking reactions. The peptide is composed entirely of natural amino acids and exhibits a marked (42%) change in fluorescence between its oxidized and its reduced states. The probe is easily synthesized and highly water soluble and exhibits well-behaved kinetics on reduction with the reductant tris-carboxyethylphosphine. The reduced peptide is an excellent substrate of the enzyme quiescin-sulfhydryl oxidase and may find utility in the characterization of other disulfide oxidoreductases.
Cline
Daniel J
DJ
Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716-2522, USA.
Thorpe
Colin
C
Schneider
Joel P
JP
D000595:Amino Acid Sequence; D005456:Fluorescent Dyes / Q000138:chemical synthesis* / Q000737:chemistry; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D013050:Spectrometry, Fluorescence; D013879:Thioredoxins / Q000737:chemistry; D050862:Oxidoreductases Acting on Sulfur Group Donors
D005456:Fluorescent Dyes; D010088:Oxidoreductases; D010455:Peptides; D013879:Thioredoxins; D050862:Oxidoreductases Acting on Sulfur Group Donors