Date of Award
Union College Only
Bachelor of Science
chain, PFAAs, binding, HSA, model
A novel model for measuring the strength of peruoroalkyl acid (PFAA) binding to human serum albumin (HSA) using the protein's native uorescence is described. The model is derived from published properties of HSA and its interactions with other surfactants; it is consistent with these properties and experimental observations. The model's validity has been tested with both medium- to long-chain PFAAs (peruoroheptanoate, peruorooctanoate, peruorononanoate, peruorodecanoate, peruoroundecanoate, peruorohexane sulfonate, and peruorooctane sulfonate) and short-chain PFAAs (peruorohexanoate and peruorobutane sulfonate). These experiments con_rm the model as a valid description for the binding of medium- to long-chain PFAAs to HSA. Results indicate at least 2-3 PFAAs bind to each protein with a_nity on the order of 104 M�1. Binding strengths demonstrate dependence upon peruorocarbon chain length, ionic head group, and protein concentration. The model is not valid for the binding of short-chain PFAAs to HSA. Hill binding coe_cients, uorescence intensity measurements, and wavelengths of maximum emission suggest short-chain PFAAs associate with HSA di_erently and fail to promote the same conformational changes in the protein's tertiary structure as the medium- to long-chain PFAAs.
Hebert, Paul C., "A novel fluorescence model for studying the binding of medium- to long-chain per uoroalkyl acids to human serum albumin" (2010). Honors Theses. 1149.