Transanalysis of Human Serum Albumin Function Based On Evolutionarily and Experimentally Unique Amino Acids

Open Access
Artello, Sean Richard
Area of Honors:
Biology (Behrend)
Bachelor of Science
Document Type:
Thesis Supervisors:
  • Michael A Campbell, Thesis Supervisor
  • Michael A Campbell, Honors Advisor
  • Paul Edward Barney Jr., Faculty Reader
  • Human serum albumin
  • Oxygen binding
  • Oxidative stress
  • Genetic analysis
  • Multiple species
  • Jalview
  • Clustal Omega alignment
  • Phylogeny
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.