Date of Award
5-11-2025
Date Published
June 2025
Degree Type
Thesis
Degree Name
Master of Science (MS)
Department
Biomedical and Chemical Engineering
Advisor(s)
Shikha Nangia
Keywords
Claudin-16;Claudins;Homodimer;Kidney disease;PANEL;Tight junctions
Subject Categories
Chemical Engineering | Engineering
Abstract
Claudin-16 is a member of the Claudin family of proteins, which play a critical role in establishing paracellular permeability within tight junctions between cells. Claudin-16 exhibits diverse properties related to ion selectivity, tissue development, and barrier function. Depending on the context, claudins create channels that permit the passage of specific ions through the paracellular space or form barriers that restrict ion movement. This study focuses on the self-assembly of the human claudin-16 protein, which is essential for ion reabsorption and the proper functioning of the kidney. Molecular simulations were employed to investigate the interactions within dimerized claudin-16 and to elucidate its role in ion selectivity, using both atomistic and coarse-grained approaches. The self-assembly of claudin-16 was characterized using the Protein AssociatioN Energy Landscape (PANEL) tool, which generated energy landscape plots that captured the population density, minimum interaction energies between transmembrane segments, and residue-to-residue contacts within the system. This computational analysis highlights the importance of in silico methods for uncovering detailed protein-protein and residue-residue interactions, offering a significant advancement over traditional in vitro techniques.
Access
Open Access
Recommended Citation
Atimah, Baqi Ozomata, "IN-SILICO INVESTIGATION OF CLAUDIN-16 SELF ASSEMBLY IN TIGHT JUNCTIONS" (2025). Theses - ALL. 931.
https://surface.syr.edu/thesis/931
