Kinetics of the inhibition of calmodulin-dependent protein kinase II by pea protein-derived peptides
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Notice bibliographique
Résumé
Calmodulin (CaM) is a ubiquitous protein present in all living cells and is involved in calcium-mediated activation of various physiologically important enzymes.Agents that bind to CaM can prevent activity of CaM-dependent protein kinase ll (CaMKll), an enzyme that has been implicaied in the initiation and propagation of chronic diseases.Agents that decrease or block the activity of CaMKll can reduce or eliminate excessive protein phosphorylation and, therefore, minimize or prevent associated pathological conditions.lnhibitors of CaM usually have either a net positive charge or a net hydrophobic character.Therefore, pea protein isolate with high levels of positively charged amino acids was enzymatically hydrolyzed to generate peptides with net positive charges.The peptides were separated on a cation-exchange column to obtain two peptide fractions that differed in level of positive charges.CaM-binding determination showed that fraction #2 had higher contents of basic amino acid residues and almost three times affinity for CaM when compared with fraction #1 .Enzyme inhibition kinetics was studied for peptides to see if they could inhibit CaMKll activity.lnhibition by the two peptide fractions followed a competitive manner and fraction #2 had a higher inhibition constant than fraction #1 .Fluorescence spectrophotometry and circular dichroism (CD) were used to determine the structural changes of CaM in the presence of enzyme and inhibitory peptides.The results showed thai interactions between CaM and inhibitory peptides led to the unfolding of CaM and exposure of previously buried hydrophobic groups.Peptide #2 was more effective than peptide #1 in causing unfolding of CaM.CD studies showed that the inhibitory peptides reduced the amount of c-helix siructure, a conformation that seems to be required for optimum interaction of CaM with target enzymes.Excessive unfolding of CaM by the inhibitory peptides led to increased interaction with CaMKll followed by unfolding of enzyme structure and reduction in enzyme activity.lt was concluded that pea protein-derived low molecular weight peptides with net positive charges interacted strongly and caused excessive unfolding of CaM, which reduced the ability of CaM to activate CaMKll; howeve this inhibition can be removed by increasing the concentrations of CaM. ACKNOWLEGMENTFirst and foremost, I would sincerely like to thank my
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Scores Codex et Gemma par catégorie
| Catégorie | Codex | Gemma |
|---|---|---|
| Métarecherche | 0,000 | 0,000 |
| Méta-épidémiologie (sens strict) | 0,000 | 0,000 |
| Méta-épidémiologie (sens large) | 0,000 | 0,000 |
| Bibliométrie | 0,000 | 0,000 |
| Études des sciences et des technologies | 0,001 | 0,001 |
| Communication savante | 0,000 | 0,000 |
| Science ouverte | 0,000 | 0,000 |
| Intégrité de la recherche | 0,000 | 0,000 |
| Charge utile insuffisante (le modèle a refusé de juger) | 0,000 | 0,000 |
Scores machine (provisoires)
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score_only:v0-immature-baseline · tel quel depuis la passe de notation : score_only signifie que le nombre peut ordonner les travaux, et qu'aucune étiquette de catégorie n'en découle