Revealing the structural dynamics of feline serum albumin
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ORIGINAL RESEARCH
Revealing the structural dynamics of feline serum albumin Prapasiri Pongprayoon 1,2
&
Deanpen Japrung 3
Received: 25 May 2020 / Accepted: 18 August 2020 # Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract Serum albumin (SA) is a prevalent carrier protein in blood. SA carries a diverse range of nutrients, drugs, and metal ions. It has wide clinical and biochemical applications. In veterinary use, human serum albumin (HSA) was administered to increase albumin level and osmotic pressure in critically ill dogs and cats, but this therapy is very expensive and under debate. Using other albumins is one of the alternatives for a cross-species usage. Thus, understanding structural dynamics of albumins from other animals becomes essential. In this work, feline serum albumin (FSA) is computationally studied in comparison with bovine (BSA), canine (CSA), and human (HSA) serum albumins from a previous work for the first time. FSA shares high sequence identity to CSA, but its dynamics resembles HSA and BSA. Like other albumins, the different movement of domains I and III is a signature of each albumin. FSA shows similar size of Sudlow site I to BSA and HSA, whereas its Sudlow site II is smaller. This permits the different drug-binding affinity of FSA at Sudlow site II. Furthermore, C34 in FSA is more flexible than HSA due to no interaction with Y84 that anchors C34 on a protein surface. An increased flexibility of C34 thiol group can easily trigger undesired thiolation or dimerization. Although FSA shares similar dynamics to HSA, its different ligand-binding affinity can be a key weakness to serve as a HSA substitute in cross-species animals. Keywords Feline serum albumin . FSA . MD simulations
Abbreviations FSA Feline serum albumin BSA Bovine serum albumin CSA Canine serum albumin HSA Human serum albumin MD Molecular dynamics
Electronic supplementary material The online version of this article (https://doi.org/10.1007/s11224-020-01619-4) contains supplementary material, which is available to authorized users. * Prapasiri Pongprayoon [email protected] * Deanpen Japrung [email protected] 1
Department of Chemistry, Faculty of Science, Kasetsart University, Chatuchak, Bangkok 10900, Thailand
2
Center for Advanced Studies in Nanotechnology for Chemical, Food and Agricultural Industries, KU Institute for Advanced Studies, Kasetsart University, Bangkok 10900, Thailand
3
National Nanotechnology Center, National Science and Technology Development Agency, Thailand Science Park, Pathumthani 12120, Thailand
Introduction Serum albumin (SA) is the most abundant protein in plasma. It plays multiple roles in physiology including acting as a carrier for drugs, fatty acids, metal ions, and metabolites and maintaining osmotic pressure. A study of SA with small molecules has come into light due to a wide range of clinical, biochemical, and pharmaceutical applications [1]. Human serum albumin (HSA) has been widely studied as drug carriers [2, 3] and diagnostic biomarkers for many diseases
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