Comparative Studies on the Interaction of Spermidine with Bovine Trypsin by Multispectroscopic and Docking Methods

Momeni, Lida; Shareghi, Behzad; Saboury, Ali Akbar; Farhadian, Sadegh

doi:10.1021/acs.jpcb.6b06648

Cited by 47 publications

(3 citation statements)

References 46 publications

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“…To confirm the hypothesis that LOS and FUR can interact not only with HSA but also with each other, spectrophotometric measurements were performed. The mutual interactions were also analyzed by Momeni et al and Ren et al [ 30 , 31 ]. They studied the interaction between spermidine and bovine trypsin, as well as trypsin and resveratrol.…”

Section: Resultsmentioning

confidence: 99%

Comparison of Losartan and Furosemide Interaction with HSA and Their Influence on HSA Antioxidant Potential

et al. 2022

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Serum albumin (HSA) is the most important protein in human body. Due to the antioxidant activity, HSA influences homeostasis maintenance and transport of drugs as well as other substances. It is noteworthy that ligands, such as popular drugs, modulate the antioxidant activity of HSA. The aim of this study was to analyze the influence of losartan (LOS) and furosemide (FUR) on HSA antioxidant properties as well as the interaction between these drugs and protein using calorimetric and spectroscopic methods. LOS and FUR showed the high affinity for human serum albumin, and the binding reactions between them were spontaneous and exothermic. LOS and FUR, separately and together in the system, have no significant impact on the secondary HSA structure; however they have significant impact on the tertiary HSA structure. LOS and FUR mixed with HSA have the ability to scavenge free radicals, and the ligand(s)–HSA interactions were synergistic.

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Section: Resultsmentioning

confidence: 99%

Comparison of Losartan and Furosemide Interaction with HSA and Their Influence on HSA Antioxidant Potential

et al. 2022

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“…The number of the binding site was equal to unity, suggesting that one independent site on BSA was available for the ligand molecule. Various similar instances were accessible in the literature, giving the number of the binding site on protein for ligand [33,34,38,[44][45][46][47][48][49]. The linear coefficient R 2 (0.99) depicts that the assumption underlying the derivation of equation (3) was satisfactory.…”

Section: G Rtlnk 5 B ( ) D = -mentioning

confidence: 99%

Spectroscopic investigation on the interaction of direct yellow-27 with protein (BSA)

Bisht¹,

Dey²,

Singh³

et al. 2022

Methods Appl. Fluoresc.

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Direct yellow 27 (DY-27) interaction with bovine serum albumin (BSA) was investigated using multi-spectroscopic techniques to understand the toxicity mechanism. Fluorescence quenching of BSA by DY-27 was observed as a result of the formation of a BSA-DY27 complex with a binding constant of 1.19 × 105 M-1 and followed a static quenching mechanism with a quenching constant Ksv of 7.25 × 104 M-1. The far UV circular dichroism spectra revealed the conformational changes in the secondary structure of BSA in the presence of DY-27. The calculated average lifetime of BSA is 6.04 ns and is nearly constant (5.99 ns) in the presence of dye and supports the proposed quenching mechanism. The change in free energy (ΔG) was calculated to be -28.96 kJ mol-1 and confirmed the spontaneity of the binding process. Further, docking studies have been conducted to gain more insights into the interactions between DY-27 and serum albumin.

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“…[13] It is an endopeptidase that can catalyze the hydrolytic cleavage of digestive bonds near hydrophobic or aromatic amino acid residues. [14,15] Trypsin and α-chymotrypsin are both serine proteases, [16,17] which are produced as zymogen cells in the pancreas of the duodenum. [18] These three enzymes can specifically break down the connections between specific types of amino acids during the digestion process, resulting in the breakdown of dietary proteins into their constituent parts.…”

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Interaction between caffeic acid phenethyl ester and protease: monitoring by spectroscopic and molecular docking approaches

et al. 2022

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The interaction of one anticancer drug (caffeic acid phenethyl ester; CAPE) with three proteases (trypsin, pepsin and α-chymotrypsin) has been investigated with multispectral methods and molecular docking. As an active components in propolis, the findings are of great benefit to metabolism, design, and structural modification of drugs. The results show that CAPE has an obvious ability to quench the trypsin, pepsin, or α-chymotrypsin fluorescence mainly through a static quenching procedure.Trypsin has the largest binding affinity to CAPE, and α-chymotrypsin has the smallest binding affinity to CAPE. The data obtained from thermodynamic parameters and molecular docking prove that the spontaneously interaction between CAPE and each protease is mainly due to a combination of van der Waals (vdW) force and hydrogen bond (H-bond), controlled by an enthalpy-driven process. The binding force, strength, position, and the number of H-bond are further obtained from the results of molecular docking. Through ultraviolet spectroscopy, dynamic light scattering and circular dichroism experiments, the change in the protease secondary structure induced by CAPE was observed. Additionally, the addition of protease had a positive effect on the antioxidative activity of CAPE, and α-chymotrypsin has the greatest effect on the removal of 2,2-diphenyl-1-picrylhydrazyl free radicals by CAPE.α-chymotrypsin, caffeic acid phenethyl ester (CAPE), pepsin, trypsin | INTRODUCTIONCaffeic acid phenethyl ester (CAPE) has been widely used in various regions as a traditional natural medicine. [1] As the main active ingredient of propolis, CAPE has various biological activities, including anticancer, anti-inflammatory, antibacterial, neuroprotective, etc. [2][3][4] In addition, it has a very strong antioxidant capacity, [5] as a polyphenol containing hydroxyl groups in benzenediol. [6] In previous works, the study of the interaction between CAPE and macromolecules mainly focus on the binding mechanism, influencing factors, drug activities, and pharmacology; many theoretical researches have been done.Studies have shown that poly(3-hydroxybutyrate) (PHB) fibre can enhance the antioxidant and antibacterial activities of CAPE. [7] CAPE can inhibit iNOS gene transcription by inhibiting the nuclear factor NF-κB site, and can inhibit the catalytic activity of iNOS, [8] which provides a research basis for the anti-inflammatory and antitumour effects of CAPE. According to reports, after CAPE is compounded with γ-cyclodextrin (γ-CD), the anticancer activity of CAPE will increase. [9] In addition, in the work of this research group, the binding constant of CAPE and bovine serum albumin was $10 6 , of which the main forces are H-bond and vdW force, and the driving mode is enthalpy drive. However, there are few studies on the interaction

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Comparative Studies on the Interaction of Spermidine with Bovine Trypsin by Multispectroscopic and Docking Methods

Cited by 47 publications

References 46 publications

Comparison of Losartan and Furosemide Interaction with HSA and Their Influence on HSA Antioxidant Potential

Comparison of Losartan and Furosemide Interaction with HSA and Their Influence on HSA Antioxidant Potential

Spectroscopic investigation on the interaction of direct yellow-27 with protein (BSA)

Interaction between caffeic acid phenethyl ester and protease: monitoring by spectroscopic and molecular docking approaches

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