2012
DOI: 10.1016/j.jff.2012.03.007
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Changes in arterial blood pressure after single oral administration of cuttlefish (Sepia officinalis) muscle derived peptides in spontaneously hypertensive rats

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Cited by 22 publications
(3 citation statements)
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“…ACE inhibition is the main mechanism by which peptides can modulate RAS function and exert antihypertensive effects. A number of in vivo studies performed in animals and/or humans have demonstrated that various food-derived peptides could significantly reduce blood pressure through ACE inhibition upon either intravenous or oral administration [ 93 , 94 , 95 , 96 , 97 , 98 , 99 , 100 ]. Milk protein derived peptides are known for their antihypertensive activity.…”
Section: Antihypertensive Peptides From Food Proteins—mechanisms Omentioning
confidence: 99%
“…ACE inhibition is the main mechanism by which peptides can modulate RAS function and exert antihypertensive effects. A number of in vivo studies performed in animals and/or humans have demonstrated that various food-derived peptides could significantly reduce blood pressure through ACE inhibition upon either intravenous or oral administration [ 93 , 94 , 95 , 96 , 97 , 98 , 99 , 100 ]. Milk protein derived peptides are known for their antihypertensive activity.…”
Section: Antihypertensive Peptides From Food Proteins—mechanisms Omentioning
confidence: 99%
“…The kinetic constants of competitive and non-competitive ACE inhibitory peptides indicate a decrease in V max as the concentration of inhibitor increases . Peptides isolated from collagen hydrolysates exhibit competitive ACE inhibitory activity . Research by Memarpoor-Yazdi et al showed that egg white lysozyme-derived peptide inhibited ACE activity in a non-competitive manner, indicating an interaction with the enzyme protein outside the active site.…”
Section: Discussionmentioning
confidence: 99%
“…37 Peptides isolated from collagen hydrolysates exhibit competitive ACE inhibitory activity. 38 Research by Memarpoor-Yazdi et al 39 showed that egg white lysozyme-derived peptide inhibited ACE activity in a non-competitive manner, indicating an interaction with the enzyme protein outside the active site. ACE inhibitory peptide (Val-Glu-Cys-Tyr-Gly-Pro-Asn-Arg-Pro-Gln-Phe) isolated from the pepsin hydrolysate of algae protein waste from Chlorella vulgaris was found to have an IC 50 value of 29.6 μM against ACE as a non-competitive inhibitor.…”
Section: ■ Discussionmentioning
confidence: 99%