Date of Award

2011

Degree Type

Thesis

Degree Name

Master of Science

Program

Biochemistry

Supervisor

Dr. Gilles Lajoie

Abstract

Pin1 is an enzyme essential to cell cycle regulation and has a key role in cancer proliferation. This thesis reports ongoing efforts to obtain a Pin1 inhibitor exhibiting an inhibition constant in the nanomolar range.

It was previously found that Pin 1 activity could be inhibited using a short proline containing peptide sequence which also contains a stereospecific (3- substituted a-amino acid. Several proline analogues were tested for greater inhibition against Pin1 than previously synthesized Cbz-/_-Glu((3-phos)-Pro-NH2. It was found that using full length Pin1 in the chymotrypsin-coupled photometric assay rendered different values than using only the catalytic PPIase domain for Cbz-Z_-Glu((3-phos)-Pro-NH2, Kj = 54.1+1.8 pM and 20 ± 0.9 pM respectively. The potential effectiveness of the synthesized inhibitors against Pin1 was assessed using the same convenient chymotrypsin-coupled photometric assay against full length Pin1.

This thesis describes the synthesis of two novel compounds which exhibited an increase in inhibition relative to Cbz-/_-Glu((3-phos)-Pro-NH2(Kj = 54.1+1.8 pM) with results in the micromolar range; Cbz-Z_-Glu(f3-phos)-Pip-NH2 (Kj = 45.4+1.1 pM) and Cbz-/_-Glu(p-phos)-Methylpiperazine (Kj = 22.7+1.4 pM)

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