ABSTRACT
Objectives: Serum albumin [SA] is one of the most abundant proteins in human plasma and performs functions for protein transport, scavenges for free radicals, and regulates osmotic pressure. SA has been used for therapy in humans with several diseases including hypovolemia, hypoalbuminemia, and chronic liver disease. However, the most appropriate source of albumin for medical applications remains unclear, especially in the case of viral infections, which complicates finding viable donors. Substitution of human serum albumin [HSA] with albumin from other natural sources is a viable alternative. Therefore, we elucidated the similarity in character, structure and evolutionary relationship among serum albumin isolated from seven different species
Methods: We compared the sequence, structure, and properties of SA from different species using an in-silico approach
Results: These data suggested that SA has sequence polymorphism that clusters based on closely relatedspecies. However, these polymorphisms do not change the three-dimensional structure of the protein; this may serve to maintain its function as a transporter. The Gallus gallus albumin has the lowest number of the epitopes that closely resemble HSA
Conclusion: This study is crucial in providing explicit information about the structural similarity of albumin isolated from other species compared to HSA. The Gallus gallus SA might be used as a primary natural source of albumin where warranted for human therapy