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- W2890760151 abstract "The interaction between trelagliptin and pepsin was probed through spectroscopy methods and molecular dynamics simulation. Results of fluorescence lifetime and fluorescence spectroscopy analysis showed that trelagliptin can spontaneously interact with pepsin through a static quenching. This interaction was mainly driven by hydrogen bonding and van der Waals, as evident from thermodynamic parameters and molecular dynamics simulation. The microenvironment of tyrosine residues and the secondary structure of pepsin were slightly influenced by trelagliptin based on synchronous fluorescence, three-dimensional fluorescence, and circular dichroism spectra. In addition, the activity of pepsin was hardly affected by the insertion of trelagliptin. Molecular dynamics simulations were used to further analyze the pepsin–trelagliptin complex. This study provides useful information for binding mechanisms of trelagliptin on pepsin." @default.
- W2890760151 created "2018-09-27" @default.
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- W2890760151 date "2018-08-09" @default.
- W2890760151 modified "2023-10-11" @default.
- W2890760151 title "Interaction between trelagliptin and pepsin through spectroscopy methods and molecular dynamics simulation" @default.
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- W2890760151 doi "https://doi.org/10.1080/00387010.2018.1469154" @default.
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