Interaction between trelagliptin and pepsin through spectroscopy methods and molecular dynamics simulation

Suo, Zili; Ma, Xiaodong; Meng, Zhihan; Du, Qiaohong; Li, Hui

doi:10.1080/00387010.2018.1469154

Cited by 5 publications

(1 citation statement)

References 43 publications

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“…Pepsin is one of the important enzymes involved in the digestive system and is used as a model of proteases in interaction studies with small molecules. Due to the highly acidic residue, pepsin with an optimum pH is 1.5-2.0 is a monomeric L-protein consisting of two structurally homologous domains [20][21][22]. Trypsin is a proteolytic enzyme that breaks down peptide bonds in the carboxylic groups of arginine, lysine and ornithine and has an optimum pH of 7.5-8.5.…”

Section: Introductionmentioning

confidence: 99%

Evaluation of the Binding Properties of A New Phenylurea Appended Carbazole Compound to Pepsin/Trypsin by Computational and Multi-Spectral Analysis

Gökoğlu

Doyuran

Özen

et al. 2023

Preprint

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A novel carbazole compound, named 1-(9-ethyl-9H-carbazol-3-yl)-3-phenylurea (Cpu) was synthesized and its binding properties with protease enzymes (pepsin and trypsin) has been examined by steady-state fluorescence measurements, UV/vis absorption, infrared (FT-IR) and circular dicroism (CD) spectroscopies and also computational methods. The fluorescence experimental results indicated that the quenching mechanism of enzyme by Cpu is static process. The thermodynamic parameters (both negative ΔH/ΔS) and molecular docking results suggested that the binding of Cpu to pepsin/trypsin were driven by hydrogen bonds and van der Waals forces. Based on Förster’s theory, the binding distance (r) between pepsin/trypsin and Cpu was calculated to be 3.072/2.784 nm, which implies that non-radiative energy transfer occurs from enzyme to Cpu. Furthermore, absorption, CD, and FT-IR spectral analysis provided an evidence that the presence of Cpu induced notable changes in the secondary structures and microenvironmental of both pepsin and trypsin, supporting its significant influence on these enzymes.

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Section: Introductionmentioning

confidence: 99%

Evaluation of the Binding Properties of A New Phenylurea Appended Carbazole Compound to Pepsin/Trypsin by Computational and Multi-Spectral Analysis

Gökoğlu

Doyuran

Özen

et al. 2023

Preprint

View full text Add to dashboard Cite

show abstract

Evaluation of the Binding Properties of A New Phenylurea Appended Carbazole Compound to Pepsin/Trypsin by Computational and Multi-Spectral Analysis

Gökoğlu,

Doyuran,

Özen

et al. 2023

J Fluoresc

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A novel carbazole compound, named 1-(9-ethyl-9H-carbazol-3-yl)-3-phenylurea (Cpu) was synthesized and its binding properties with protease enzymes (pepsin and trypsin) has been examined by steady-state uorescence measurements, UV/vis absorption, infrared (FT-IR) and circular dicroism (CD) spectroscopies and also computational methods. The uorescence experimental results indicated that the quenching mechanism of enzyme by Cpu is static process. The thermodynamic parameters (both negative ΔH/ΔS) and molecular docking results suggested that the binding of Cpu to pepsin/trypsin were driven by hydrogen bonds and van der Waals forces. Based on Förster's theory, the binding distance (r) between pepsin/trypsin and Cpu was calculated to be 3.072/2.784 nm, which implies that non-radiative energy transfer occurs from enzyme to Cpu. Furthermore, absorption, CD, and FT-IR spectral analysis provided an evidence that the presence of Cpu induced notable changes in the secondary structures and microenvironmental of both pepsin and trypsin, supporting its signi cant in uence on these enzymes.

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The interaction between troxerutin and pepsin was studied by multispectral method and molecular docking simulation

Wang,

Sun,

Nie

et al. 2024

Journal of Molecular Structure

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Interaction between trelagliptin and pepsin through spectroscopy methods and molecular dynamics simulation

Cited by 5 publications

References 43 publications

Evaluation of the Binding Properties of A New Phenylurea Appended Carbazole Compound to Pepsin/Trypsin by Computational and Multi-Spectral Analysis

Evaluation of the Binding Properties of A New Phenylurea Appended Carbazole Compound to Pepsin/Trypsin by Computational and Multi-Spectral Analysis

Evaluation of the Binding Properties of A New Phenylurea Appended Carbazole Compound to Pepsin/Trypsin by Computational and Multi-Spectral Analysis

The interaction between troxerutin and pepsin was studied by multispectral method and molecular docking simulation

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