Olga V. Makhlynets
Assistant Professor
Chemistry & Biochemistry
Education
Ph.D
Tufts University - 2011
M.S. & B.S.
National Taras Shevchenko University of Kyiv, Ukraine - 2004 & 2003
Postdoctoral Researcher
Massachusetts Institute of Technology - 2011 - 2013
Experience
Assistant Professor of Chemistry
Syracuse University - 2014 - 2023
Assistant Professor of Chemistry
Baylor University - 2024 - Present
Research
Manganese homeostasis in S. pneumoniae: My research program focuses at the interface between chemistry and biology. We use bioinorganic chemistry and microbiology approaches to study how human pathogen Streptococcus pneumoniae controls manganese levels inside the cell. Specifically, we target two proteins, one involved in manganese acquisition when this element is not easily available and another protein is responsible for removing excess manganese from the intracellular space. Since regulation of manganese levels is critical for the ability of S. pneumoniae to cause disease, this research may ultimately lead to new therapeutics.
Antimicrobial hydrogels: Another project aims to design peptide-based antimicrobial hydrogels. Infections associated with methicillin-resistant Staphylococcus aureus (MRSA), E. coli, P. aeruginosa, and Candida species have become a common problem in hospitals. Antimicrobial gels emerged as one of the strategies to prevent or treat such infections and have been designed in form of wound fillers, implant coating and for drug delivery. We study how sequence length and hydrophobic component of peptide as well as metal ion presence influence properties of the resulting hydrogel.
Protein design: We redesign small and stable non-enzymatic proteins to catalyze useful chemical reactions, such as ester hydrolysis and acylation. Most recent work focused on modulating pKa value of a catalytic histidine and measuring how this change influences catalytic efficiency. This work involves a series of NMR experiments in combination with a straightforward computational analysis, and provides guidance to rationally improve catalytic efficiency of histidine-promoted catalysis.