First direct fluorination of tyrosine-containing biologically active peptides

✍ Scribed by D. Hebel; K.L. Kirk; L.A. Cohen; V.M. Labroo

• Publisher: Elsevier Science
• Year: 1990
• Tongue: French
• Weight: 253 KB
• Volume: 31
• Category: Article
• ISSN: 0040-4039
• DOI: 10.1016/s0040-4039(00)94583-0

✦ Synopsis

Abstracti Using acetyl hypoflurite a regiospecific electrophilic fluorination of the tyrosine ring of the N-terminal tetrapeptide amide (Tyr-D-Ala-Phe-Gly-NH,) sequence of the opiate peptide dermorphin has been achieved in good yields. Fluorinated analogues of biologically active compounds are important biochemical and pharmacological agents.' Fluoro compounds often mimic their nonfluorinated parents with respect to enzyme and receptor recognition, yet can drastically change the potency and receptor selectivity of the molecule.2 In addition, fluorinated molecules have been used as markers that can be unequivocally detected using either 19F NMR3 or energy loss spectroscopic techniques.' Furthermore, a variety of '*F labelled compounds are finding increasing application in positron emission tomography (PET).' Consequently, there is a constant need and search for new, efficient and relatively fast ways to introduce fluorine into biologically important molecules. Although many methods have been developed for fast and efficient incorporation of