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Analysis of Drug-protein Interactions on Modified Proteins During Diabetes and Use of Immunoextraction for Personalized Medicine
Human serum albumin (HSA) is the most abundant protein in serum and is responsible for the transportation and distribution of various small molecules in blood, such as fatty acids, hormones and drugs. HSA is known to be important in the regulation, distribution and metabolism of many drugs and in determining the effectiveness of these drugs in patients. Additionally, it is known that HSA can be altered due to numerous diseases, which can impact its structure and function. One such example is type II diabetes, in which HSA can be altered through a process known as glycation. Glycation is a process by which proteins are modified in the presence of glucose, leading to structural and functional changes in proteins. Aside from causing modifications to HSA, glycation can lead to the formation of the advanced glycated end-products (AGEs), which may also affect drug-protein interactions. The work presented in this dissertation is focused on the use of immunoextraction to study drug-protein interactions between sulfonylurea drugs with normal and AGE-modified HSA, as well as the use of immunoextraction for the isolation and entrapment of HSA from human serum for drug-protein studies with sulfonylurea drugs, as related to personalized medicine.
Rodriguez, Elliott L, "Analysis of Drug-protein Interactions on Modified Proteins During Diabetes and Use of Immunoextraction for Personalized Medicine" (2019). ETD collection for University of Nebraska - Lincoln. AAI22587211.