Identification of peptides in wheat germ hydrolysate that demonstrate calmodulin-dependent protein kinase II inhibitory activity

Transport, Bioavailability, Safety, and Calmodulin-Dependent-Phosphodiesterase-Inhibitory Properties of Flaxseed-Derived Bioactive Peptides

“…Because CaM acts by binding to and thus changing the conformation of target proteins, ligands that can bind and modify CaM conformation could potentially influence many CaM-mediated cellular reactions and may be used to design therapeutic agents . Previous studies have identified CaM as a potential target of specific bioactive peptides as well as protein hydrolysates from food sources like casein, wheat, pea, and flaxseed. − For instance, low-molecular-weight cationic peptide fractions obtained after ion-exchange chromatography of ultrafiltered pea-protein hydrolysates were demonstrated as showing a strong affinity for CaM, thus resulting in considerable inhibition of CaMKII activity . By inhibiting the activities of CaM-dependent protein kinases, phosphodiesterases, and nitric oxide synthases, CaM-binding peptides could be used to control or manage pathological conditions that are associated with anomalous activities of these enzymes.…”