wileyonlinelibrary.com/journal/jms
Journal of
Volume 49 Number 4
April 2014
MASS
SPECTROMETRY
Featured article
(wileyonlinelibrary.com) DOI 10.1002/jms.3269
Proteomic analysis of peptides tagged with dimedone and related probes
P. Martínez-Acedo, V. Gupta and K. S. Carroll
Pages 257–265
Protein sulfenylation (-SOH), the redox-based modification of cysteine thiol side
chains by hydrogen peroxide (H2O2), is emerging as an important mechanism in
signal transduction. Dysregulated protein sulfenylation contributes to a range
of human pathologies. However, efforts to elucidate the diverse roles of protein
sulfenylation in physiology and disease have, to date, suffered from the lack
of reliable techniques to detect these modifications. The chemoselective
reactivity of dimedone (5,5-dimethyl-1,3-cyclohexanedione) toward –SOH has
been exploited to detect protein sulfenic acids by mass spectrometry, but its
utility has been questioned by some groups. In this Special Feature, Dr MartínezAcedo and co-workers use a combination of targeted and high-throughput
proteomic approaches to solve the questions regarding the possible ionization
inhibition issues and fragmentation behavior of dimedone-based probes. Their
findings suggest that dimedone is a suitable tool for the identification of the
great unknowns of the sulfenylome.
The blue Vitruvian Man image was used with permission from AlphaAnatomy.
Authors’ biographies
Pablo Martínez-Acedo earned his PhD in 2012 in Molecular Biology at Centro de Biología Molecular “Severo Ochoa” (MadridSpain) with Prof. Jesús Vázquez, where he worked on the development of O18 labeling techniques and high-throughput peptide
analysis by mass spectrometry applied to the molecular study of the dynamic state of the thiol redoxome. He is currently a
postdoctoral researcher at Scripps Florida in Dr Carroll’s group where his main research topic is the development and improvement
of proteomics workflows focused on the identification and quantification of cysteine sulfenic acids in biological environments.
Vinayak Gupta received his Ph.D. in Organic Chemistry from Iowa State University under the supervision of Prof.
George A. Kraus where his research focused on methodology development and total syntheses of natural products.
After graduating in 2010, he joined the laboratory of Dr Carroll at Scripps Florida to work towards the sulfenic acid probe
development.
Kate S. Carroll is an Associate Professor in the Department of Chemistry at The Scripps Research Institute in Jupiter, Florida.
She received her B.A. degree in Biochemistry from Mills College in 1996 and Ph.D. in Biochemistry from Stanford University in
2003. Her postdoctoral work was completed at the University of California, Berkeley with Prof. Carolyn Bertozzi. She was an
Assistant Professor at the University of Michigan until 2010, when she joined the Chemistry faculty at Scripps. Her research
interests span the disciplines of chemistry and biology with an emphasis on studies of sulfur biochemistry pertinent to disease
states. Her lab focuses on the development of novel tools to study redox modifications of cysteine thiols, profiling changes
in protein oxidation associated with disease, and exploiting this information for development of diagnostic and therapeutic
approaches.