Resume

• 2004

  New York University

  University of Tampa

  H. Lee Moffitt Cancer Center and Research Institute

  My postdoctoral work investigated the mechanisms of cell adhesion mediated drug resistance (CAM-DR) in multiple myeloma with classical biology and innovative mass spectrometry based techniques.\n\nI expanded my knowledge base in mass spectrometry from characterization of peptide integrity to advanced mass spectrometry based proteomics techniques which in turn were used to identify novel protein-protein interactions.\n\nI researched the modulation of signal transduction pathways that affect cell adhesion mediated drug resistance (CAM-DR)

  specifically Bim and AMPK. Through this work I developed skills in mammalian cell culture

  and cell biology techniques including western blotting

  immunoprecipitation

  and qPCR.

  Postdoctoral Research Fellow

  Tampa/St. Petersburg

  Florida Area

  H. Lee Moffitt Cancer Center and Research Institute

  In my current role

  I support the educational goals of the department by teaching a standard faculty teaching load in organic chemistry (lab & lecture). Additionally

  I supervise and provide leadership to a core group of undergraduate students employed in the chemistry department as organic chemistry mentors (undergraduate TA’s). \n\nI provide guidance to senior level students in scientific writing and presenting during a senior seminar course. Teaching the seniors student about scientific writing is one of the more enjoyable activities I have experienced as an educator.\n\nAs the manager of the organic chemistry laboratory

  I have a variety of duties including editing and compiling manuals

  maintaining lab equipment

  and updating chemical inventory.\n\nI am often trusted to edit manuscripts

  abstracts

  and sabbatical applications for faculty members.

  Organic Chemistry Lecturer/Lab Coordinator

  Tampa/St. Petersburg

  Florida Area

  University of Tampa

  My graduate work focused mainly on chemical biology and peptidomimetic research to target protein-protein interactions that are of interest in cancer progression. I became an expert in the design

  synthesis and characterization of peptides and peptidomimetics. I evaluated the affinity of my compounds for a specific protein (that I overexpressed and purified from E. coli) with fluorescence polarization techniques. \n\nMy work led to several publications in scientifically peer reviewed journals including the Proceedings of the National Academy of Sciences (PNAS) and the Journal of the American Chemical Society (JACS). I collaborated with other groups throughout the country and analyzed compounds through circular dichroism and fluorescence polarization which afforded another JACS publication. \n\nI was also an active member of the chemistry department through the graduate student council and as a teaching assistant. I was author on a publication in the Journal of Chemical Education through the Honors Organic Laboratory. I also authored an invited mini-review for Current Opinions in Chemical Biology.\n

  Graduate Research Assistant

  Greater New York City Area

  New York University

  WO2010033879 A3

  American Chemical Society

  Responsible for writing the quarterly newsletter to 700+ ACS members

  Secretary of Tampa Bay Section - 2015

  SAACS participates in a number of outreach events throughout the course of the year. As co-advisor to the group

  I coordinate some of the outreach events to promote chemistry within the community. The group volunteered at the Glazer Children's Museum during National Chemistry Week for the past 3 years.

  Co-advisor

  Student Affiliates of the American Chemical Society

  Member

  Cheeky Scientist Association

  Member

  American Medical Writers Association

  Doctor of Philosophy (Ph.D.)

  Doctoral Dissertation

  \"Mimicking Alpha-Helical Transactivation Domains with Hydrogen Bond Surrogate Derived Artificial Alpha-Helices\"

  Chemistry

  Chemistry Graduate Student Council - Vice President (2007-2008)

  New York Academy of Sciences

  Laboratory of Molecular Recognition and Synthesis

  New York University

  Master of Science (M.S.)

  Department of Chemistry Excellence in Teaching Award (2006)

  Chemistry

  New York University

• 2000

  Bachelor of Science (B.S.)

  Undergraduate Thesis

  \"Synthesis of Carbohydrate Macrolactones\"\n

  Chemistry

  National Society of Collegiate Scholars

  \nGolden Key International Honors Society

  University of South Florida

• IR

  Fluorescence

  HPLC

  Peptide Synthesis

  Oncology

  Scientific Writing

  Presentations

  NMR

  Protein Chemistry

  Protein Purification

  Chemistry

  Data Analysis

  Protein Expression

  LC-MS

  UV/Vis

  Scientific Editing

  Molecular Biology

  Mass Spectrometry

  Organic Chemistry

  Biochemistry

  Protein domain mimetics as in vivo modulators of hypoxia-inducible factor signaling

  Nathaniel J. Traaseth

  Hannah Mesallati

  Ramin Dubey

  Swati Kushal

  Proceedings of the National Academy of Sciences

  Protein–protein interactions are attractive targets for interfering with processes leading to disease states. Proteins often use folded domains or secondary structures to contact partner proteins. Synthetic molecules that mimic these domains could disrupt protein–protein contacts

  thereby inhibiting formation of multiprotein complexes. This article describes protein domain mimetics (PDMs) that modulate interactions between two proteins that control expression of a multitude of genes under hypoxic environments

  such as those found inside tumors. The low-oxygen conditions promote angiogenesis—process of formation of new blood vessels—that together with invasion and altered energy metabolism facilitates tumor growth. We find that the PDMs can control expression of target hypoxia-inducible genes in cell culture and reduce tumor burden in mice.

  Protein domain mimetics as in vivo modulators of hypoxia-inducible factor signaling

  Emmanuelle J. MeuilletB

  Zuohe Song

  Joshua Makhoul

  Csaba F. Laszlo

  Swati Kushal

  Ramin Dubey

  Nathan W. Polaske

  Lajos Z. Szabo

  Hui Wang

  Katherine M. Block

  Journal of the American Chemical Society

  Selective blockade of hypoxia-inducible gene expression by designed small molecules would prove valuable in suppressing tumor angiogenesis

  metastasis and altered energy metabolism. We report the design

  synthesis

  and biological evaluation of a dimeric epidithiodiketopiperazine (ETP) small molecule transcriptional antagonist targeting the interaction of the p300/CBP coactivator with the transcription factor HIF-1α. Our results indicate that disrupting this interaction results in rapid downregulation of hypoxia-inducible genes critical for cancer progression. The observed effects are compound-specific and dose-dependent. Controlling gene expression with designed small molecules targeting the transcription factor-coactivator interface may represent a new approach for arresting tumor growth.

  Direct inhibition of hypoxia-inducible transcription factor complex with designed dimeric epidithiodiketopiperazine

  Paramjit S. Arora

  Bogdan Z. Olenyuk

  Ross N. Chapman

  Ramin Dubey

  Swati Kushal

  Designed ligands that inhibit hypoxia-inducible gene expression could offer new tools for genomic research and

  potentially

  drug discovery efforts for the treatment of neovascularization in cancers. We report a stabilized α-helix designed to target the binding interface between the C-terminal transactivation domain (C-TAD) of hypoxia-inducible factor 1α (HIF-1α) and cysteine-histidine rich region (CH1) of transcriptional coactivator CBP/p300. The synthetic helix disrupts the structure and function of this complex

  resulting in a rapid downregulation of two hypoxia-inducible genes (VEGF and GLUT1) in cell culture.

  Inhibition of hypoxia inducible factor 1 - transcription coactivator interaction by a hydrogen bond surrogate alpha-helix

  Andrea L. Jochim

  Herein we review contemporary synthetic and protein design strategies to stabilize the alpha-helical motif in short peptides and miniature proteins. Advances in organometallic catalyst design

  specifically for the olefin metathesis reaction

  enable the use of hydrocarbon bridges to either crosslink side chains of specific residues or mimic intramolecular hydrogen bonds with carbon-carbon bonds. The resulting hydrocarbon-stapled and hydrogen bond surrogate alpha-helices provide unique synthetic ligands for targeting biomolecules. In the protein design realm

  several classes of miniature proteins that display stable helical domains have been engineered and manipulated with powerful in vitro selection technologies to yield libraries of sequences that retain their helical folds. Rational re-design of these scaffolds provide distinctive reagents for the modulation of protein-protein interactions.

  Contemporary strategies for the stabilization of peptides in the alpha-helical conformation

  Donald Wink

  James Canary

  Adam Waxman

  An experiment for the undergraduate chemistry laboratory in which students perform the aldol condensation on an unknown aldehyde and an unknown ketone is described. The experiment involves the use of techniques such as TLC

  column chromatography

  and recrystallization

  and compounds are characterized by 1H NMR

  GC–MS

  and FTIR. This experiment provides the students with a thorough exercise in the practical aspects of organic chemistry. It requires students to think like researchers and allows them the opportunity to independently apply previously learned techniques in the laboratory.

  Synthesis and characterization of aldol condensation products from unknown aldehydes and ketones: an inquiry-based experiment in the undergraduate laboratory

  Paramjit S. Arora

  Indraneel Ghosh

  Jason R. Porter

  Synthetic helices target chosen protein–protein interactions with high specificity

  as assessed by an in vitro split-protein reassembly assay. By using the p53/MDM2 complex as a model system

  both the efficacy of the designed ligands and the suitability of the split-protein assay were determined.

  High specificity in protein recognition by hydrogen-bond-surrogate alpha-helices: selective inhibition of the p53/MDM2 complex

  Laura

  Henchey