Design of active-site-directed fluorescent probes and their reactions with biopolymers

✍ Scribed by Himel, Chester M. ;Mayer, Richard T. ;Cook, Larry L.

• Book ID: 104535424
• Publisher: Wiley (John Wiley & Sons)
• Year: 1970
• Tongue: English
• Weight: 547 KB
• Volume: 8
• Category: Article
• ISSN: 0449-296X
• DOI: 10.1002/pol.1970.150080828

✦ Synopsis

Abstract

Fluorescent probes which are active‐site‐directed, reversible, competitive inhibitors of serum cholinesterase (ChE) enzymes have been designed and synthesized. Reversible inhibitors of enzyme active sites have a unique importance when they act as fluorescent probes, allowing fluorescence spectroscopic detection of conformation changes and activesite dynamics. 5‐Dimethylamino‐naphthalene‐1‐sulfonamido‐N,N‐dimethyl‐n‐propyl‐amine and its aliphatic quaternary derivative are fluorescent probes for serum cholinesterase. The quaternary probe forms complexes with acetylcholinesterase (AChE). The dissociation constants K~d~ for the two probes with serum ChE are 6.0 × 10^−7^ and 6.5 × 10^−7^M. The inhibition constants K~i~ are 3.1 × 10^−6^ and 6.3 × 10^−6^M from the slopes of Lineweaver‐Burk plots. The Michelis constant K~m~ for the enzyme was 8.8 × 10^−4^M.