Structural Properties of Rat Intestinal Fatty Acid-Binding Protein with its
Dynamics: Insights into Intrinsic Disorder

Oyku   Irem   Balli; Sule   Irem   Caglayan; Vladimir   N.   Uverksy; Orkid      Coskuner-Weber

doi:10.2174/0109298665313811240530055004

Abstract

Background: The rat intestinal fatty acid-binding protein (I-FABP) is expressed in the small intestine and is involved in the absorption and transport of dietary fatty acids. It is used as a marker for intestinal injury and is associated with various gastrointestinal disorders. I-FABP has been studied extensively using conventional experimental and computational techniques. However, the detection of intrinsically disordered regions requires the application of special sampling molecular dynamics simulations along with certain bioinformatics because conventional computational and experimental studies face challenges in identifying the features of intrinsic disorder.

Methods: Replica exchange molecular dynamics simulations were conducted along with bioinformatics studies to gain deeper insights into the structural properties of I-FABP. Specifically, the Cα and Hα chemical shift values werecalculated, and the findings were compared to the experiments. Furthermore, secondary and tertiary structure properties were also calculated, and the protein was clustered using k-means clustering. The end-to-end distance and radius of gyration values were reported for the protein in an aqueous solution medium. In addition, its disorder tendency was studied using various bioinformatics tools.

Results and Conclusion: It was reported that I-FABP is a flexible protein with regions that demonstrate intrinsic disorder characteristics. This flexibility and intrinsic disorder characteristics of IFABP may be related to its nature in ligand binding processes.

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DOI https://dx.doi.org/10.2174/0109298665313811240530055004	Print ISSN 0929-8665
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Structural Properties of Rat Intestinal Fatty Acid-Binding Protein with its Dynamics: Insights into Intrinsic Disorder

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