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Dynamic and structural properties of porcine serum albumins
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Document Title
Dynamic and structural properties of porcine serum albumins
Author
Niramitranon J., Japrung D., Boonmee A., Koonawootrittriron S., Suwanasopee T., Jattawa D., Pongprayoon P.
Affiliations
Faculty of Engineering, Department of Computer Engineering, Kasetsart University, Bangkok, Thailand; National Nanotechnology Center, National Science and Technology Development Agency, Thailand Science Park, Pathumthani, Thailand; Faculty of Science and Technology, Department of Chemistry, Rambhai Barni Rajabhat University, Chanthaburi, Thailand; Faculty of Agriculture, Department of Animal Science, Kasetsart University, Bangkok, Thailand; Faculty of Science, Department of Chemistry, Kasetsart University, Bangkok, Thailand; Faculty of Science, Computational modelling unit for Food Health and Agriculture (ComFHA), Department of Chemistry, Kasetsart University, Bangkok, Thailand; Center for Advanced Studies in Nanotechnology for Chemical, Food and Agricultural Industries, KU Institute for Advanced Studies, Kasetsart University, Bangkok, Thailand
Type
Article
Source Title
Molecular Simulation
ISSN
08927022
Year
2023
Page
-
Open Access
All Open Access, Green
Publisher
Taylor and Francis Ltd.
DOI
10.1080/08927022.2023.2200485
Format
Abstract
Porcine 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. © 2023 Informa UK Limited, trading as Taylor & Francis Group.
Publication Source
WOS