Chemical and Enzymatic Synthesis of Dehydropeptides and Their Fluoro Analogs

Fluorine-substituted dehydroalanine can lead to irreversible linkages of nucleophile to dehydroalanines by an addition elimination mechanism and can be applied to the design of enzyme inhibitors and active site affinity labels. Fluorodehydroalanine has been synthesized from serine in 7 steps with a fluoro-Pummerer rearrangement as the key step. The stereochemical integrity at the alpha-carbon in the fluoro-Pummerer rearrangement was investigated and proven to be retained. Furthermore, dehydropeptides and their fluoro analogs were prepared in an enzymatic fashion. For instance, fluorinated dipeptides, L-alanine-D-fluoroalanine and L-alanine- D,L-difluoroalanine were treated with the epimerase YcjG to produce L-Ala-Dha and L-Ala-Dha(F), respectively, as determined by 1H NMR, 19F NMR and MS (ESI).

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Chemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Zhou, Hao

Contributors dc:contributor

• van der Donk, Wilfred A.

• Chemistry, Organic

Language dc:language

eng

Identifier

(MiAaPQ)AAI3070494

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84097