Transanalysis of Human Serum Albumin Function Based On Evolutionarily and Experimentally Unique Amino Acids
Open Access
- Author:
- Artello, Sean Richard
- Area of Honors:
- Biology (Behrend)
- Degree:
- Bachelor of Science
- Document Type:
- Thesis
- Thesis Supervisors:
- Michael A Campbell, Thesis Supervisor
Michael A Campbell, Thesis Honors Advisor
Paul Edward Barney Jr., Faculty Reader - Keywords:
- Human serum albumin
Oxygen binding
Oxidative stress
Genetic analysis
Multiple species
Jalview
Clustal Omega alignment
Phylogeny - Abstract:
- Human serum albumin (HSA) is a predominant blood protein with binding affinity to many endogenous and exogenous compounds. Following an overview of this protein, the additional capacity for heme binding is analyzed as both an evolutionarily retained and experimentally inducible function. An inclusive analysis of HSA has examined all facets of HSA’s current structure, potential variations of this structure that may be induced experimentally, and the potential for evolutionary selection regarding beneficial variance. Initial background information was analyzed including structure and function, the role of HSA within the body, and medical applications, including a proposal for protein modification to facilitate the new application of heme binding and oxygen carrying ability. Once these variations were reviewed, 10 different species (mammalian, reptilian, and avian) were examined for conserved or new heme binding functionality within five relevant heme binding regions. Analysis at these regions, positions 138, 142, 146, 161, and 190 showed relative conservation, but the potential for heme binding as an accommodation for oxidative stress appears negligible within these species. Following this evaluation, procedure and methodology was outlined for the generation of mutant HSA plasmid and possible routes of generating mutant HSA protein with heme binding capability.