Person: Edson, Cody
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https://www.husson.edu/directory/cody_edson
Term at University
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Assistant Professor, College of Science and Humanities
Last Name
Edson
First Name
Cody
Name
Degrees Held
Ph.D. Chemistry, 2022, Rensselaer Polytechnic Institute
M.S. Chemistry, 2017, Southern Connecticut State University
B.S. Chemistry, 2016, Southern Connecticut State University
M.S. Chemistry, 2017, Southern Connecticut State University
B.S. Chemistry, 2016, Southern Connecticut State University
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Publication SEED IT OR LEAVE IT: A LOOK AT CELL SEEDING EFFECTS ON TISSUE ENGINEERED VASCULAR GRAFTS(2026-04-16) Hinton, Thomas; Villarreal, Delaney; Reinhardt, James; Turner, Mackenzie; Briggs, Mitchell; Hussein, Jad; Leland, Joseph T.; Rajesh, Sahana; Suravarapu, Sugath; Watanabe, Tatsuya; Humphrey, Jay; Ramachandra, Abhay; Breuer, Christopher; Edson, CodyCongenital heart disease is one of the most common causes of birth defect mortalities in infants. Reconstructive surgery is often the only form of treatment yet causes life-long complications for survivors. The reconstructive Fontan operation for congenital heart disease currently uses synthetic polytetrafluoroethylene (PTFE) vascular grafts. Although effective, PTFE grafts pose risks such as calcification and thrombosis, and cannot grow with the patient, which may necessitate multiple surgical interventions and ultimately affect long-term outcomes. Tissue engineered vascular grafts (TEVGs) are a promising alternative to PTFE grafts. TEVGs consist of a biodegradable polymer scaffold, which fully degrades within one year after implantation, leaving behind a neovessel formed from the patient’s own cells. Most importantly, TEVG neovessels can grow with the patient and self-repair, like native tissue. The main clinical complication precluding widespread adaptation of the TEVG is graft narrowing, or stenosis, which was determined to be inflammation driven. Currently, clinical TEVGs are seeded with the patient’s bone marrow mononuclear cells (BM-MNCs), which are believed to reduce graft immunogenicity and potentially reduce the incidence and severity of stenosis. However, this approach limits scalability in clinical settings and adds yet another operative procedure for the patients. Our goal is to understand the short- and long-term effects of cell seeding on TEVG neovessel growth and development. For this study, we assessed TEVG growth and degree of narrowing longitudinally with biomedical imaging in a large-animal ovine model. We determined that unseeded TEVGs had the same development profiles as cell seeded TEVGs. This suggests that we may be able to remove the need for cell seeding procedures in our clinical trial without compromising any aspect of TEVG development and remodeling. * - Husson University + - Center for Regenerative Medicine, The Abigail Wexner Research Institute at Nationwide Children’s HospitalPublication ALPHA-CHYMOTRYPSIN PROTEASE-CATALYZED PEPTIDE SYNTHESIS OF ALTERNATING ARGNINE-TRYPTOPHAN PEPTIDES AND THEIR ANTIMICROBIAL PROPERTIES(2026-04-16) Lessa, Timothy; Edson, CodyAntimicrobial peptides (AMPs) are an increasingly popular topic in research due to their effectiveness against drug-resistant bacteria and pathogens. These peptides target the cell membrane of the bacteria and that makes them very difficult for bacteria to build resistance to. Due to this, AMPs are being developed to help treat viral infections, aid in wound healing, act as a safe preservative for agriculture, and could be used to target cancer cells. The conventional synthesis methods for antimicrobial peptides however often involve harsh chemicals, large amounts of waste, and high costs. Therefore, to investigate more environmentally and economically favorable synthesis strategies for AMPs we used an alternative synthesis method in Protease-Catalyzed Peptide Synthesis (PCPS). PCPS is conducted using water as a solvent and is relatively cheaper, uses less toxic reagents, and utilizes renewable protease enzymes as catalysts. We specifically sought to form a repeating Arginine-Tryptophan amino acid sequence because of tryptophan’s ability to anchor to a cell wall and arginine’s ability to destroy it, making them a great antimicrobial agent. The protease enzyme I chose to investigate this synthesis with is Alpha-Chymotrypsin, because while it favors the hydrolysis of Tryptophan-Arginine amide bonds, we can target the reverse aminolysis reaction by using Arginine-Tryptophan dipeptide units which interact with the active sight of the enzyme differently and favor aminolysis over hydrolysis. We predict that the Alpha-Chymotrypsin will yield a bell-curve like distribution of alternating peptide chains ranging from 2-16 amino acids in length, which is the typical range of amino acid chain length for PCPS reactions. We will also conduct an antimicrobial assay to determine the oligopeptide’s effectiveness against gram + and gram -bacteria and determine the minimum inhibition concentration.Publication ANTIBACTERIAL EFFICACY AND SACCHARIDE COMPOSITION OF HONEY DETERMINED BY MICROBIAL ASSAYS AND GC-MS(2026-04-16) Beaulieu, Sierra; Edson, CodyHoney is a food product that has been used for centuries as a natural remedy. In light of growing concern regarding antibacterial resistance, honey has been investigated as an antibacterial agent. This presentation considered the efficacy of honey as an antibacterial agent and quantified biochemical properties that may allow honey to be used as an alternative therapy. To determine this, testing began by utilizing an agar disc diffusion method to determine how different types of honey inhibited the growth of bacteria, these included E. coli, P. aeruginosa, and B. subtilis. No significant differences were observed between the two honey types, where a raw honey product and a commercially available honey were each tested. Further analysis was conducted to determine a minimum inhibitory concentration of honey, where each honey type was diluted 10-fold in a 96-well plate containing an E. coli and B. subtilis culture. Further testing was performed to deduce what biochemical properties contribute to the antimicrobial characteristics of honey. A two-step derivatization process allowed gas chromatography-mass spectrometry (GC-MS) to be used as the main method to identify saccharides in honey samples by utilizing retention index values compared to a set standard. Further testing was performed to calculate the exact concentrations of fructose, glucose, and sucrose in each honey sample. Additional testing on the heavy metal contents of honey was also carried out as a means to further compare the raw and commercially available honeys, along with their antibacterial efficacy. Together, these methods help determine the value of honey as an alternative therapy. This presentation highlights the need for further research on alternative antibacterials and provides a foundation for methods and possible antimicrobial agents.Publication PAPAIN-CATALYZED SYNTHESIS OF ALTERNATING ARGININE-TRYPTOPHAN PEPTIDES FOR ANTIMICRIOBIAL APPLICATIONS(2026-04-16) Nichols, Kaleb; Edson, CodyAntimicrobial peptides represent a promising strategy for combating multidrug resistant pathogens. However, the conventional synthesis strategy using Solid Phase Peptide Synthesis (SPPS) relies on harsh reagents, extensive solvent use and costly, multi-step protocols. In this study, we investigate a greener and more efficient approach to synthesizing peptides using Protease-Catalyzed Peptide Synthesis (PCPS) to generate short arginine-tryptophan (Arg-Trp) peptides, molecules known to possess antimicrobial properties. We examine the enzymatic coupling of Arg-Trp dipeptides using papain, a well-documented protease, as a biocatalyst under mild conditions, promoting peptide bond formation through aminolysis rather than hydrolysis. The reaction products are characterized by MALDI-TOF mass spectrometry to assess peptide formation and composition. This approach aims to provide a cost-effective and environmentally sustainable alternative to traditional peptide synthesis, with findings that will inform future studies on alternative syntheses and antimicrobial efficacy of Arg–Trp peptides produced via PCPS.