Dr. Ray Syvitski, Ph.D

Appointments:

Biomolecular Research Officer at NRC, Adjunct professor at Dalhousie University in Chemistry, and Biochemistry & Molecular Biology.

Affiliations:

National Research Council of Canada – Institute for Marine Biosciences, Dalhousie University Facility of Graduate Studies

Research Interests:

Magnetic resonance, membrane-protein interactions, chemical biology, structure/function relationship

Molecular Structure, Binding & Tracking of Cancer Drugs

Utilizing various magnetic resonance (MR) techniques such as spectroscopy and imaging, we investigate how drugs function by determining structure, identifying essential parts components necessary for activity and tracking the movement of drugs within a living organism. By identifying the structure and essential components, it may be possible to modify drugs to (for example) change activity or specificity. MRI is used to determine if drugs are targeting cancer cells and/or affecting other organs/tissues within organisms.

Membership Status:

Dr. Syvitski is a BHCRI Associate Member.

Phone:

(902) 426-1674

Email:

Ray.Syvitski@nrc-cnrc.gc.ca

Address:

NRC, Biomolecular Magnetic Resonance Facility, Room 158, 1411 Oxford St, Halifax, NS, B3H 3Z1

Publications:

A Novel Target-Specific, Salt-Resistant Antimicrobial Peptide against the Cariogenic Pathogen Streptococcus mutans Junni Mai, Xiao-Lin Tian, Jeffrey W. Gallant, Nadine Merkley, Zakia Biswas, Raymond Syvitski, Susan E. Douglas, Junqi Ling, and Yung-Hua Li. Antimicrob. Agents Chemother. (2011) 55 5205-5213

Cell-Cell Membrane Fusion Induced by the p15 Fusion-Associated Small Transmembrane (FAST)
Protein Requires a Novel Fusion Peptide Motif Containing a Myristoylated Polyproline Type II Helix.
Deniz Top, Jolene A. Read, Sandra J. Dawe, Raymond T. Syvitski, and Roy Duncan. J. Biol. Chem. (2011) 287 3403-3414

A method for structure-activity analysis of quorum-sensing signaling peptides from naturally transformable streptococci. Tian X, Syvitski RT, Liu T, Livingstone N, Jakeman DL, Li YH. Biol Proced Online. (2009) 11 207-26.

Expression, purification and structural characterization of recombinant hepcidin, an antimicrobial peptide identified in Japanese flounder, Paralichthys olivaceus. Srinivasulu, B.; Syvitski, Raymond. T.; Seo, J.-K.; Mattatall, N. R.; Knickle, L. C.; Douglas, S. E. Protein Expres Purif. (2008) 61(1) 36-44.

Strategies for recombinant expression of small, highly disulphide-bonded, cationic antimicrobial peptides. Greenshields, A. L.; Knickle, L. C.; Syvitski, Raymond T.; Douglas, S. E. Protein Peptide Lett (2008) 15(9) 985-994

Enzyme-catalyzed synthesis of furanosyl nucleotides. Timmons, Shannon C.; Hui, Joseph P. M.; Pearson, Jessica L.; Peltier, Pauline; Daniellou, Richard; Nugier-Chauvin, Caroline; Soo, Evelyn C.; Syvitski, Raymond T.; Ferrieres, Vincent; Jakeman, David L. Org. Lett. (2007) 10(2), 161-163.

Sterochemical Integrity of Oxazolone Ring-Containing Jodomycins. Borissow, Charles N.; Graham, Cathy L.; Syvitski Raymond T.; Reid, Taryn R.; Blay, Jonathan; Jakeman, David L. ChemBioChem (2007) 8(10), 1198-1203.

Structure-Activity Analysis of Synthetic Quorum-Sensing Signal Peptides from Streptococcus mutans. Syvitski, Raymond T.; Tian, Xiao-Lin; Sampara, Kamal; Salman, Alan; Lee, Song F.; Jakeman, David L.; Li, Yung-Hua. J. Bacteriolog. (2006) 189(4), 1441-1450.

Substrate Flexibility of a 2,6-dideoxyglycosyltransferase. Jakeman, David L.; Borrissow, Charles N.; Graham, Cathy L.; Timmons, Shannon; Reid, Taryn R.; Syvitski, Raymond T. Chem. Comm.(2006), 3738-3740.