2019
DOI: 10.1016/j.jmgm.2019.03.019
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An anticoagulant peptide from Porphyra yezoensis inhibits the activity of factor XIIa: In vitro and in silico analysis

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Cited by 10 publications
(4 citation statements)
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“…The MM/PBSA method calculated the drug's target-protein receptor binding free energy. Molecular mechanics potential energy (electrostatic and van der Waals interaction) and free energy of solvation (polar and nonpolar solvation energies) are used to estimate binding energy from dynamic trajectories [57].…”
Section: In Silico Studymentioning
confidence: 99%
“…The MM/PBSA method calculated the drug's target-protein receptor binding free energy. Molecular mechanics potential energy (electrostatic and van der Waals interaction) and free energy of solvation (polar and nonpolar solvation energies) are used to estimate binding energy from dynamic trajectories [57].…”
Section: In Silico Studymentioning
confidence: 99%
“…yezoensis (NMEKGSSSVVSSRMKQ) and the coagulation factor XIIa. The study reported that interactions of this peptide with factor XIIa were through hydrogen bonds [113]. Molecular docking of peptides derived from U. intestinalis , FGMPLDR, and MELVLR, indicated that these peptides were able to bind to the active site of ACE through a network of hydrogen bonds and hydrophobic and Van der Waals interactions, and that glycine (G) and Leucine (L) residues within the peptides disturb the Zn(II) ion within ACE potentially resulting in inhibition of the enzyme activity [103].…”
Section: In Silico Analysismentioning
confidence: 99%
“…Marine products generally exhibit particular scaffolds not found in terrestrial sources [168,169]. From the hydrolysate of marine organisms, two FXIIa inhibitors were reported: the 12-kDa yellowfin sole anticoagulant protein [170] and the 16-mer peptide VITPOR AI (IC50 in plasma = 70.24 µM) [171,172].…”
Section: Discovery From Marine Organismsmentioning
confidence: 99%