Scholars@Duke
Peter Silinski

Peter Silinski

Research Associate, Senior
Chemistry
peter.silinski@duke.edu
Box 90354, Durham, NC 27708-0354
124 Science Drive, Box 90354, French Family Science Center, Room 2325, Durham, NC 27708

Selected Publications

Resveratrol Protects Against Hydroquinone-Induced Oxidative Threat in Retinal Pigment Epithelial Cells.

Journal Article Invest Ophthalmol Vis Sci · April 9, 2020 PURPOSE: Oxidative stress in retinal pigment epithelial (RPE) cells is associated with age-related macular degeneration (AMD). Resveratrol exerts a range of protective biologic effects, but its mechanism(s) are not well understood. The aim of this study wa ... Full text Open Access Link to item Cite

Synthesis and physicochemical characterization of (6S)-5-formiminotetrahydrofolate; a reference standard for metabolomics

Journal Article Organic & Biomolecular Chemistry · 2018 The coenzyme (6S)-5-formiminotetrahydrofolate, has been prepared by reaction of (6S)-tetrahydrofolate with ethyl formimidate and thoroughly physicochemically characterized. Conditions for storage and handling of this se ... Full text Cite

Process Development of TRI-999, a Fatty-Acid-Modified HIV Fusion Inhibitory Peptide

Journal Article Organic Process Research & Development · January 1, 2008 Full text Cite

Theoretical and experimental determination on two substrates turned over by 4-oxalocrotonate tautomerase.

Journal Article The journal of physical chemistry. A · January 2006 Quantum mechanical/molecular mechanical (QM/MM) calculations and experimental kinetic studies have been performed on 4-oxalocrotonate tautomerase (4OT) for two different substrates, 2-hydroxymuconate (2HM) and 2-oxo-4-hexenedioate (2o4hex). Potential (delt ... Full text Cite

The protein backbone makes important contributions to 4-oxalocrotonate tautomerase enzyme catalysis: understanding from theory and experiment.

Journal Article Biochemistry · June 2004 The role of polypeptide backbone interactions in 4-oxalocrotonate tautomerase (4OT) catalysis has been investigated using a combination of site-directed mutagenesis experiments with unnatural amino acids and quantum mechanical/molecular mechanical (QM/MM) ... Full text Cite

Comparative analysis of two different amide-to-ester bond mutations in the beta-sheet of 4-oxalocrotonate tautomerase.

Journal Article Biochemistry · June 2003 Here we describe the total chemical synthesis and biophysical characterization of two backbone-modified, ester bond-containing analogues of the homohexameric enzyme 4-oxalocrotonate tautomerase (4OT). The amide-to-ester bond mutations in the two analogues ... Full text Cite

A stable dimer in the pH-induced equilibrium unfolding of the homo-hexameric enzyme 4-oxalocrotonate tautomerase (4-OT).

Journal Article Biochemistry · April 2002 4-Oxalocrotonate tautomerase (4-OT) is a multimeric, bacterial enzyme comprised of 6 identical 62-amino acid subunits, which associate under native conditions to form a homo-hexameric structure stabilized entirely by noncovalent interactions. We have previ ... Full text Cite

Guanidine-induced equilibrium unfolding of a homo-hexameric enzyme 4-oxalocrotonate tautomerase (4-OT).

Journal Article Biochemistry · April 10, 2001 4-Oxalocrotonate tautomerase (4-OT) is a bacterial enzyme that is comprised of 6 identical 62 amino acid subunits. The 4-OT enzyme is an attractive model system in which to study the interrelationship between protein folding, subunit assembly, and catalyti ... Full text Link to item Cite

Identification of an essential backbone amide bond in the folding and stability of a multimeric enzyme

Journal Article Journal of the American Chemical Society · August 30, 2000 Here we utilize a total chemical synthesis strategy and a mass spectrometry-based, combinatorial chemistry approach to identify key molecular interactions that contribute to the folding and stability of a model multimeric enzyme, 4-oxalocrotonate tautomera ... Cite