Angiotensin-I converting enzyme (ACE) inhibitory mechanism of tripeptides containing aromatic residues

Kobayashi, Yuka; Yamauchi, Tadashi; Katsuda, Tomohisa; Yamaji, Hideki; Katoh, Shigeo

doi:10.1263/jbb.106.310

Cited by 42 publications

(31 citation statements)

References 6 publications

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“…The changes in ACE FI reflects K i values as reported in Table 1, which indicates binding affinity increased from TF to LY. The stronger binding effects of LY and RALP may be due to the fact that these peptides contain both bulky and hydrophobic amino acids, which are known to enhance hydrophobic interactions between enzymes and ligands [21]. The results (decreases in FI upon interaction with peptides) indicate partial unfolding of ACE protein structure to produce a more open conformation than the native structure.…”

Section: Resultsmentioning

confidence: 99%

Evaluating Molecular Mechanism of Hypotensive Peptides Interactions with Renin and Angiotensin Converting Enzyme

Aluko

2014

PLoS ONE

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Our previous study showed that three rapeseed protein-derived peptides (TF, LY and RALP) inhibited the in vitro activities of angiotensin converting enzyme (ACE) and renin. Oral administration of these peptides to spontaneously hypertensive rats led to reductions in systolic blood pressure. In the present work, we examined the potential molecular mechanisms responsible for the ACE- and renin-inhibitory activities of these peptides. Enzyme inhibition kinetics showed competitive, non-competitive and mixed-type peptide-dependent inhibition of renin and ACE activities. Intrinsic fluorescence intensity data showed that LY and RALP have stronger binding effects on ACE molecule compared to that of TF. LY and RALP showed the highest inhibition of ACE and renin activities, respectively. Circular dichroism data showed that the inhibitory mechanism involved extensive peptide-dependent reductions in α-helix and β-sheet fractions of ACE and renin protein conformations. Molecular docking studies confirmed that the higher renin-inhibitory activity of RALP may be due to formation of several hydrogen bonds (H-bonds) with the enzyme’s active site residues. The rapeseed peptides inhibited renin and ACE activities mostly through binding to enzyme active site or non-active sites and forming extensive H-bonds that distorted the normal configuration required for catalysis. Data presented from this work could enhance development of highly potent antihypertensive natural peptides or peptidomimetics.

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Section: Resultsmentioning

confidence: 99%

Evaluating Molecular Mechanism of Hypotensive Peptides Interactions with Renin and Angiotensin Converting Enzyme

Aluko

2014

PLoS ONE

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“…Previous studies found that peptides with low molecular weight showed higher reactivity than those with high molecular weight in the Maillard reaction . Many studies showed that peptides with high inhibition of ACE had aromatic amino acid or hydrophobic amino acid residues at their terminals . The peptides with molecular weight less than 1000 Da were absorbed by the gastrointestinal tract more easily, and then achieved their biological functions in the human body …”

Section: Resultsmentioning

confidence: 99%

Improvement of ACE inhibitory activity of casein hydrolysate by Maillard reaction with xylose

Meng

2014

J. Sci. Food Agric.

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“…Previous structure‐activity studies of ACE‐inhibitory peptides indicated the importance of aromatic, hydrophobic, and positively charged amino acid residues in determining their inhibitory potency against ACE (Wu and others 2006). It is thought that aromatic amino acid residues in the peptide sequence could block access of the substrate to the active site of ACE, whereas the presence of hydrophobic and positively charged amino acids could enhance the binding to ACE (Miguel and others 2004; Kobayashi and others 2008). Similarly, the presence of aromatic, positively charged, and hydrophobic amino acid residues in the peptide are important in contributing to the radical‐scavenging capacity of peptides through donating hydrogen to reactive oxygen species (ROS).…”

Section: Introductionmentioning

confidence: 99%

Angiotensin‐I Converting Enzyme Inhibitory and Antioxidant Activities of Egg Protein Hydrolysates Produced with Gastrointestinal and Nongastrointestinal Enzymes

Sun-Jong¹,

Wu²

2011

Journal of Food Science

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Egg is a well-known rich source of bioactive peptides. In this study, egg protein (egg white and egg yolk proteins) hydrolysates were produced with gastrointestinal enzymes (pepsin and pancreatin) or nongastrointestinal enzymes (thermolysin and alcalase), and fractionated by ultrafiltration and cation exchange chromatography. Angiotensin-I converting enzyme (ACE) inhibitory and antioxidant activities, amino acid composition and molecular weight distribution were studied, and the physicochemical properties were related with the bioactivities. Our results showed that egg protein hydrolysates produced with non-GI enzymes (thermolysin and alcalase) showed significantly higher ACE inhibitory activity, whereas similar or even lower antioxidative activities, than those of hydrolysates produced with GI enzymes. ACE-inhibitory activity significantly correlated with the amino acid composition, especially the proportion of positively charged amino acid, whereas antioxidant activities correlated with the proportion of low molecular weight peptides under 500 Da. Understanding the relationship between the bioactivities and physicochemical properties of the hydrolysates/fractions is important to facilitate the development technologies for preparing fractions with improved bioactivities.

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Angiotensin-I converting enzyme (ACE) inhibitory mechanism of tripeptides containing aromatic residues

Cited by 42 publications

References 6 publications

Evaluating Molecular Mechanism of Hypotensive Peptides Interactions with Renin and Angiotensin Converting Enzyme

Evaluating Molecular Mechanism of Hypotensive Peptides Interactions with Renin and Angiotensin Converting Enzyme

Improvement of ACE inhibitory activity of casein hydrolysate by Maillard reaction with xylose

Angiotensin‐I Converting Enzyme Inhibitory and Antioxidant Activities of Egg Protein Hydrolysates Produced with Gastrointestinal and Nongastrointestinal Enzymes

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