As a faculty member and scientist my goal is to serve the scientific community by
doing high-quality research in areas that impact our society—and the world. In order
to do important research in chemistry and biology, I have expanded my expertise, developed
new skills, and fostered collaboration with other research scientists around the globe.
Collaboration is an important part of my research style as I can thereby extend my
and my students’ work to address larger and more complex problems. I have been a faculty
member at SUNY Plattsburgh for 12 years. Previous to this I spent 12 years at Clarkson
University where I was a faculty member in the Chemistry and Biology Departments.
I also hold an adjunct position in the Biochemistry Department at the University of
Vermont College of Medicine.
In my research endeavors, I take a broad experimental approach to answering scientific
questions which incorporates methods of genetic engineering, molecular modeling, NMR,
titrating calorimetry, mass spectrometry, electrochemistry, fluorescence and UV spectroscopy.
I draw on my experience in graduate school, in postdoctoral positions, and in my work
at the National Laboratory. The research in my laboratory embraces both science and
technology and so my goal is to both address scientific questions and develop new
methodologies. Although my initial area of expertise and inquiry was investigating
receptor proteins using fluorine NMR I have branched out to advance research in the
area of biosensors, an area of inquiry that is and has been of interest to funders
and academic journals. My key focus in the biosensor research is to develop sensitive
and specific biosensors using genetically engineered proteins. The main goal is to
develop surfaces where these proteins can be sequestered and serve as a platform for
the detection of target chemicals. I have collaborated with a number of research groups
to explore different detection methods and methodology for embedding matrices for
proteins. These have included methodologies of electrochemistry, nanoparticles, atomic
force microscopy, quartz crystal microbalance and surface plasmon resonance. I performed
a recent innovative study developing a responsive “smart” protein hydrogel material
that can be used as a biosensor. This study serves as a proof of concept for biosensors
that can be constructed with photonic crystals embedded with genetically engineered
One of my research endeavors in the past couple of years is the development of a miniaturized
biosensor to detect glucose in human tears. This groundbreaking work with a company
named Opticology, will allow the diabetic population to monitor their glucose levels
without needles. Also this biosensor methodology is being adapted to the detection
of heavy metals in the environment.
My curiosity and enjoyment in culinary chemistry field prompted me to pursue research
in this area, namely molecular gastronomy. For my sabbatical I was able to obtain
an Erasmus Mundus Scholars Scholarship to study and pursue research work in this area
in Paris, France. I mainly resided in the laboratory of Hervé This, who is the “Father
of Molecular Gastronomy.”
One of my studies in this area is the investigation of the use of metallic nanoparticles
to distill liquids. In this study, the nanoparticles are immersed in water and can
act as efficient nanoscale generators of steam when illuminated by a Fresnel lens
and sunlight. In this project, I will further investigate the use of the solar steam
nanobubble phenomenon to distill ethanol from white wine and mash. The nanoparticles
used in previous studies have been silicon based. My lab will take a novel approach
and investigate the use of nanoparticles that have a magnetic metal covered with a
gold surface. The project has a dual purpose: 1) the investigation of a “green method”
for distillation of spirits and 2) the use of magnetic metal cored gold nanoparticles
so they can be stirred during the process, recovered after the process and reused
in subsequent distillations.
My other on-going project is the production of food from chemicals namely Note by
Note Cuisine. In essence every food is made up of a basic chemicals. In my lab the
students will investigate the construction of food using the basic chemical constituents
— which is the ultimate “cooking from scratch.” Then we will engineer some different
foods that are “never eaten before creations.”
Cai, Z., Luck, L.A., Punihaole, D., Madura, J.D., Asher, S.A. (2016) Photonic Crystal Protein Hydrogel
Sensor Materials Enabled by Conformationally Induced Volume Phase Transition. An Edge Article 6. Chemical Science 7, 4557-4562.
Luck, L. A., & Blondo, R. M. (2012). The grapes of class: Teaching chemistry concepts at a winery.
Journal of Chemical Education, 89(10), 1264–1266.
Roy, U & Luck, L.A. (2011) Cysteine residues in receptor proteins: Structural insights from two E. coli
periplasmic receptors. Journal of Chemistry and Chemical Engineering, 5, 771–777.
Andreescu, S. & Luck, L. A. (2008). Genetically engineered protein films on gold nanoparticles: A novel electrochemical
glucose biosensor. Analytical Biochemistry, 375, 282–290.
Roy, U., & Luck, L. A. (2007). Molecular modeling of estrogen receptor using molecular operating environment.
Biochemistry and Molecular Biology Education, 35(4), 238–243.
Wang, J., Luck, L. A., & Suni, I. I. (2007). Immobilization of the glucose-galactose receptor protein onto
a au electrode through a genetically engineered Cysteine residue. Electrochemical and Solid-State Letters, 10(2), 133–136.
Tripathi, A., Wang, J., Luck, L. A., & Suni, I. I. (2007). Nanobiosensor design utilizing a periplasmic E. coli receptor
protein immobilized within au/polycarbonate nanopores. Analytical Chemistry, 79(3), 1266–1270.
Baltus, R. E., Carmon, K. S., & Luck, L. A. (2007). Quartz crystal microbalance with immobilized protein receptors: Comparison
of response to ligand binding for direct protein immobilization and protein attachment
via disulfide linker. Langmuir, 23, 3990–3995.
Sokolov, I., Subba-Rao, V., & Luck, L. A. (2006). Change in rigidity in the activated form of the glucose/galactose receptor
from E. coli: A phenomenon that will be key to the development of piezoelectric biosensors.
Biophysical Journal, 90(3), 1055–1063.
Carmon, K. S., Baltus, R. E., & Luck, L. A. (2005). A biosensor for estrogenic substances using the quartz crystal microbalance.
Analytical Biochemistry, 345(2), 277–283.
Wang, J., Carmon, K. S., Luck, L. A., & Suni, I. I. (2005). Electrochemical impedance biosensor for glucose detection utilizing
a periplasmic E. coli receptor protein. Electrochemical and Solid-State Letters, 8(8), 61–64.
Carmon, K. S., Baltus, R. E., & Luck, L. A. (2004). A piezoelectric quartz crystal biosensor: The use of two single cysteine
mutants of the periplasmic E. coli glucose/galactose receptor as target proteins for
the detection of glucose. Biochemistry, 43(44), 14249–14256.
Abbott, G. L., Blouse, G. E., Perron, M. J., Shore, J. D., Luck, L. A., & Szabo, A. G. (2004). 19 F NMR studies of plasminogen sctivator inhibitor-1. Biochemistry, 43(6), 1507–1519.
Magnusson, U., Salopek-Sondi, B., Luck, L. A., & Mowbray, S. L. (2004). X-ray structures of the leucine-binding protein illustrate
conformational changes and the basis of ligand specificity. Journal of Biological Chemistry, 279, 8747–8752.
Luck, L. A., Moravan, M. J., Garland, J. E., Salopek-Sondi, B., & Roy, D. (2003). Chemisorptions
of bacterial receptors for hydrophobic amino acids and sugars on gold for biosensor
applications: A surface plasmon resonance study of genetically engineered proteins.
Biosensors and Bioelectronics, 19(3), 249–259.
Salopek-Sondi, B., Skeels, M. C., Swartz, D., & Luck, L. A. (2003). Insight into the stability of the hydrophobic binding proteins of E. coli:
Assessing the proteins for use as biosensors. Proteins: Structure, Function, and Genetics, 53(2), 273–281. doi:10.1002/prot.10485
Salopek-Sondi, B., Vaughan, M. D., Skeels, M. C., Honek, J. F., & Luck, L. A. (2003). 19 F NMR studies of the leucine-isoleucine-valine binding protein: Evidence
that a closed conformation exists in solution. Journal of Biomolecular Structure and Dynamics, 21(2), 235–246.
Salopek-Sondi, B., Swartz, D., Adams, P. S., & Luck, L. A. (2002). Exploring the role of amino acid-18 of the leucine binding proteins of E.
coli. Journal of Biomolecular Structure and Dynamics, 20(3), 381–387.
Salopek-Sondi, B., & Luck, L. A. (2002). 19F NMR study of the L-leucine-specific binding protein of Escherichia coli:
Mutagenesis and assignment of the 5-fluorotryptophan-labeled residues. Protein Engineering Design and Selection, 15, 857-861.
Senear, D. F., Mendelson, R. A., Stone, D. B., Luck, L. A., Rusinova, E., & Ross, J. B. A. (2002). Quantitative analysis of Tryptophan analogue
incorporation in recombinant proteins. Analytical Biochemistry, 300(1), 77–86.
Luck, L. A., Barse, J. L., Luck, A. M. & Peck, C. (2000). Conformational changes in the human
estrogen receptor observed by fluorine NMR. Biochemical Biophysical Research Communications, 270, 988–991.
Luck, L. A. & Johnson, C. (2000). Fluorescence and 19F NMR evidence that phenylalanine and 4-L-fluorophenylalanine
bind to the L-leucine specific receptor of E. coli. Protein Science, 9, 2573–2576.