SIRT1 activation by Taurine: in vitro evaluation, molecular docking and molecular dynamics simulation studies

KP, Arya Devi; Rao, S.J. Aditya; Martin, Asha

doi:10.1016/j.jnutbio.2022.108948

Cited by 16 publications

(9 citation statements)

References 57 publications

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“…This correlation has been previously observed in the study of KP et al 30 , where Tau was established as a positive regulator of SIRT1 activity in hepatic cells “in vitro”. Our results also agreed with previous studies in human cultured cells where homotaurine and GABA significantly increased the expression of SIRT1 31 , 32 .…”

Section: Resultssupporting

confidence: 79%

“…Resveratrol (3, 5, 4′-trihydroxystilbene), a polyphenol found in grapes and red wines, is one of the most effective SIRT1 activators 29 . Taurine (2-aminoethanesulfonic acid, Tau), Homotaurine (Htau), and the amino acid gamma aminobutyric acid (GABA), have been recently proposed as natural SIRT1 activators with possible therapeutic benefits for metabolic, age-related, and neurological disorders 30 – 32 . Besides, phlorotannin-rich natural extract from the brown seaweed Ascophyllun nodosum and polyphenol extract from Ecklonia cava have been studied for their ability to increase SIRT1 activity 33 , 34 .…”

Section: Introductionmentioning

confidence: 99%

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Taurine, homotaurine, GABA and hydrophobic amino acids content influences “in vitro” antioxidant and SIRT1 modulation activities of enzymatic protein hydrolysates from algae

Terriente-Palacios

Rubiño

Hortós

et al. 2022

Sci Rep

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Prevention and control of diseases and delaying the signs of ageing are nowadays one of the major goals of biomedicine. Sirtuins, a family of NAD+ dependent deacylase enzymes, could be pivotal targets of novel preventive and therapeutic strategies to achieve such aims. SIRT1 activating and inhibiting compounds, such as polyphenols and bioactive peptides, have been proposed to be involved in the development of many human diseases. The objective of this work was to assess and compare the antioxidant and SIRT1 modulation activities of enzymatic protein hydrolysates (EPHs) from a wide number of algae species (24 commercial samples and 12 samples harvested off the Atlantic coast of northern Spain). High antioxidant activities were observed in EPHs from red and green seaweed species. Moreover, 19 samples exhibited SIRT1 activation, while EPHs from the 16 samples were SIRT1 inhibitors. Pearson's correlation test and Principal Component Analysis revealed significant correlations between (1) total peptide and hydrophobic amino acid content in EPHs and their antioxidant activities, and (2) concentrations of taurine, homotaurine, and amino acid gamma aminobutyric acid in EPHs and their SIRT1 modulation activity.

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Section: Resultssupporting

confidence: 79%

Section: Introductionmentioning

confidence: 99%

Taurine, homotaurine, GABA and hydrophobic amino acids content influences “in vitro” antioxidant and SIRT1 modulation activities of enzymatic protein hydrolysates from algae

Terriente-Palacios

Rubiño

Hortós

et al. 2022

Sci Rep

View full text Add to dashboard Cite

show abstract

“…This correlation has been previously observed in the study of KP et al [30], where Tau was established as a positive regulator of SIRT1 activity in hepatic cells "in vitro". Our results also agreed with previous studies in human cultured cells where homotaurine and GABA signi cantly increased the expression of SIRT1 [31,32].…”

Section: Correlation Analysis and Principal Component Analysissupporting

confidence: 79%

“…Resveratrol (3, 5, 4′-trihydroxystilbene), a polyphenol found in grapes and red wines, is one of the most effective SIRT1 activators [29]. Taurine (2aminoethanesulfonic acid, Tau), Homotaurine (Htau), and the amino acid gamma aminobutyric acid (GABA), have been recently proposed as natural SIRT1 activators with possible therapeutic bene ts for metabolic, age-related, and neurological disorders [30][31][32]. Besides, phlorotannin-rich natural extract from the brown seaweed Ascophyllun nodosum and polyphenol extract from Ecklonia cava have been studied for their ability to increase SIRT1 activity [33,34].…”

Section: Introductionmentioning

confidence: 99%

Taurine, Homotaurine, GABA and hydrophobic amino acids content influences “in vitro” antioxidant and SIRT1 modulation activities of enzymatic protein hydrolysates from algae

Terriente-Palacios¹,

Campoy²,

Hortós³

et al. 2022

Preprint

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Prevention and control of diseases and delaying the signs of ageing are nowadays one of the major goals of biomedicine. Sirtuins, a family of NAD+ dependent deacylase enzymes, could be pivotal targets of novel preventive and therapeutic strategies to achieve such aims. SIRT1 activating and inhibiting compounds, such as polyphenols and bioactive peptides, have been proposed to be involved in the development of many human diseases. The objective of this work was to assess and compare the antioxidant and SIRT1 modulation activities of enzymatic protein hydrolysates (EPHs) from a wide number of algae species (24 commercial samples and 12 samples harvested off the Atlantic coast of northern Spain). High antioxidant activities were observed in EPHs from red and green seaweed species. Moreover, 19 samples exhibited SIRT1 activation, while EPHs from the 16 samples were SIRT1 inhibitors. Pearson's correlation test and Principal Component Analysis revealed significant correlations between i) total peptide and hydrophobic amino acid content in EPHs and their antioxidant activities, and ii) concentrations of taurine, homotaurine, and amino acid gamma aminobutyric acid (GABA) in EPHs and their SIRT1 modulation activity.

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“…Preceding the initiation of molecular docking, both the ligand and receptor underwent protonation and charge assignment. Molecular docking was conducted using the Auto Dock Vina 1.2.2 software, with binding energy calculations utilized to assess molecular binding activity [ 28 , 29 , 30 ]. The binding mode of patulin to the protein was visualized using Pymol 2.1 and BIOVIA Discovery Studio 4.5 software.…”

Section: Methodsmentioning

confidence: 99%

Patulin Biodegradation Mechanism Study in Pichia guilliermondii S15-8 Based on PgSDR-A5D9S1

Xi,

Wang,

et al. 2024

Toxins

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Patulin contamination has become a bottleneck problem in the safe production of fruit products, although biodegradation technology shows potential application value in patulin control. In the present study, the patulin biodegradation mechanism in a probiotic yeast, Pichia guilliermondii S15-8, was investigated. Firstly, the short-chain dehydrogenase PgSDR encoded by gene A5D9S1 was identified as a patulin degradation enzyme, through RNA sequencing and verification by qRT-PCR. Subsequently, the exogenous expression system of the degradation protein PgSDR-A5D9S1 in E. coli was successfully constructed and demonstrated a more significant patulin tolerance and degradation ability. Furthermore, the structure of PgSDR-A5D9S1 and its active binding sites with patulin were predicted via molecular docking analysis. In addition, the heat-excited protein HSF1 was predicted as the transcription factor regulating the patulin degradation protein PgSDR-A5D9S1, which may provide clues for the further analysis of the molecular regulation mechanism of patulin degradation. This study provides a theoretical basis and technical support for the industrial application of biodegradable functional strains.

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SIRT1 activation by Taurine: in vitro evaluation, molecular docking and molecular dynamics simulation studies

Cited by 16 publications

References 57 publications

Taurine, homotaurine, GABA and hydrophobic amino acids content influences “in vitro” antioxidant and SIRT1 modulation activities of enzymatic protein hydrolysates from algae

Taurine, homotaurine, GABA and hydrophobic amino acids content influences “in vitro” antioxidant and SIRT1 modulation activities of enzymatic protein hydrolysates from algae

Taurine, Homotaurine, GABA and hydrophobic amino acids content influences “in vitro” antioxidant and SIRT1 modulation activities of enzymatic protein hydrolysates from algae

Patulin Biodegradation Mechanism Study in Pichia guilliermondii S15-8 Based on PgSDR-A5D9S1

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