Cystic Fibrosis (CF) is a genetic disorder caused by a mutation in the cystic fibrosis transmembrane conductance regulator (CFTR) protein that leads to a buildup of thick and sticky mucus in the lungs, pancreas, and liver. It causes a variety of problems including persistent respiratory infection, malnutrition and infertility. Cystic Fibrosis treatments are currently limited in efficacy and cost, either treating symptoms but not the cause, or being very expensive. Cystic Fibrosis is caused by a variety of mutations, but most commonly by the AF508 mutation that stops the CFTR protein from folding correctly and limiting the expression.

N-Methylglycine, or sarcosine, is a methylated form of glycine, and an osmolyte, a group of compounds known to assist in protein folding and facilitate osmosis. The C. elegans strain OG472 has a transgenic pgp-3, a protein similar to CFTR. The OG474 strain exhibits AF508 in the transgenic pgp-3 protein. Both strains have a fluorescent tag that can be used to visualize and quantify protein levels and function. After being exposed to N-methylglycine the OG474 strain should show a higher fluorescence level and therefore more protein function.

The purpose of this research is to determine if N-methylglycine will affect the AF508 mutation and the associated Cystic Fibrosis. From this research, previous findings that C. Elegans can be used as a model will be confirmed. The C. elegans were exposed to 10mm, 5MM, 10M, and 0.1mM of N-methylgycine, just water, and nothing for three days, after standardizing stages of growth with age synchronization. After three days, the C. elegans were paralyzed and, using a Fluorescence microscope, images were taken. Only the control groups exposed to water were found to be significantly different, reaffirming that C. elegans are a feasible model for Cystic Fibrosis. Fluorescence values for all other tests were found to be insignificant implying N Methylglycine should not be used as a treatment for Cystic Fibrosis, but the data could be affected by lower numbers of images. Possible future studies include looking at other osmolytes and how they interact with the CFTR proteins.