Dynamic and structural properties of porcine serum albumins

ABSTRACTPorcine serum albumin (PSA) is one of the promising biomarkers for pork detection. Pork contamination is a serious concern for the global halal food industry since many manufacturers mix pork into halal beef products to reduce production costs. Many studies have thus been devoted to designing effective PSA-detecting biosensors. PSA is closely related to Bovine serum albumin (BSA); therefore; the molecular insight into PSA characteristics becomes crucial to identify PSA. To understand PSA properties, Molecular dynamic (MD) simulations were employed. The three-dimensional structures of PSA were obtained from homology modelling and Alphafold. Both models give similar results. PSA seems to have high hydrophobicity and unique electrostatic properties. Unlike BSA, PSA has no large electropositive patch on the rear of domain III. This property can be used to differentiate PSA from BSA. In the case of drug sites, PSA provides comparable sizes of drug sites to those of canine serum albumin (CSA) which are larger than those of bovine, human and feline albumins. Such larger binding pockets can imply the ability of PSA to accommodate a broader spectrum of ligands. The findings here, especially the difference between BSA and PSA, can serve as a base to design effective biosensors to detect PSA contaminants.KEYWORDS: Porcine serum albuminalbuminMD simulations AcknowledgementsWe also thank the NSTDA supercomputer center (ThaiSC) for computer facility support.Disclosure statementNo potential conflict of interest was reported by the author(s).Additional informationFundingThis work was supported by Kasetsart University Research and Development Institute [grant number FF(KU)3.65].