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Screening of ACE-inhibitory peptides from a random peptide-displayed phage library using ACE-coupled liposomes

Journal of Biotechnology, 2007
Angiotensin I converting enzyme (ACE)-inhibitory peptides were screened from a random peptide-displayed phage library using ACE-coupled liposomes. Among four kinds of inhibitory peptides selected by biopanning with two different elution strategies, a peptide (LSTLRSFCA) showed the highest inhibitory activity with an IC(50) value of 3microM.
Yoichi, Kumada   +6 more
openaire   +2 more sources

A novel ACE inhibitory peptide isolated from Acaudina molpadioidea hydrolysate

Peptides, 2009
Body wall protein from the sea cucumber (Acaudina molpadioidea) was hydrolyzed sequentially with bromelain and alcalase. The hydrolysate was fractionated into two ranges of molecular weight (PH-I, >2 kDa; PH-II,
Yuanhui, Zhao   +6 more
openaire   +2 more sources

Identification and the molecular mechanism of a novel myosin-derived ACE inhibitory peptide

Food & Function, 2018
The objective of this work was to identify a novel ACE inhibitory peptide from myosin using a number of in silico methods.
Zhipeng Yu   +7 more
openaire   +2 more sources

[Synthesis and activity of ACE inhibitory peptides].

Yao xue xue bao = Acta pharmaceutica Sinica, 2012
To find anti-hypertensive lead drug, angiotensin converting enzyme (ACE) inhibitory peptides were synthesized and their effects on inhibiting ACE activity were investigated. ACE inhibitory peptides were synthesized via Fmoc solid-phase synthesis, isolated and purified through reversed phase high-performance liquid chromatography (RP-HPLC), and ...
Jin, Ren   +5 more
openaire   +1 more source

Identification of Potent ACE Inhibitory Peptides from Wild Almond Proteins

Journal of Food Science, 2017
Abstract In this study, the production, fractionation, purification and identification of ACE (angiotensin‐I‐converting enzyme) inhibitory peptides from wild almond ( Amygdalus scoparia ) proteins were investigated.
Mozhgan Mirzapour   +2 more
openaire   +2 more sources

CoMFA and CoMSIA analysis of ACE-inhibitory, antimicrobial and bitter-tasting peptides

European Journal of Medicinal Chemistry, 2014
Comparative molecular field analysis (CoMFA) and comparative molecular similarity indices analysis (CoMSIA) were applied to the ACE-inhibitory, antimicrobial, and bitter-tasting peptides. Predictive 3D-QSAR models were established using SYBYL multifit molecular alignment rule over a training set and a test set. The optimum models were all statistically
Shufen, Wu   +5 more
openaire   +2 more sources

Optimisation of the hydrolysis of goat milk protein for the production of ACE-inhibitory peptides

Journal of Dairy Research, 2013
Goat milk protein was hydrolysed with subtilisin and trypsin. As input variables, temperature was assayed in the interval 45–70 °C for subtilisin and 30–55 °C for trypsin, while the enzyme-substrate ratio varied from 1 to 5%. The effect of the input variables on the degree of hydrolysis and ACE-inhibitory activity (output variables) was modelled by ...
Francisco Javier, Espejo-Carpio   +3 more
openaire   +2 more sources

Production of ace inhibitory peptides by digestion of chickpea legumin with alcalase

Food Chemistry, 2003
Abstract Short peptides from different sources have proved to be very efficient inhibitors of the angiotensin I-converting enzyme, an enzyme with a major role in the regulation of blood pressure. These peptides are of therapeutic value, so that the possibility of obtaining such peptides by treatment of chickpea legumin with the protease alcalase has ...
Marı&#x;a M. Yust   +5 more
openaire   +1 more source

Rational module substitution strategy to enhance ACE-inhibitory peptide activity

Food Chemistry
Food-derived angiotensin-converting enzyme (ACE)-inhibitory peptide plays key roles in hypertension prevention, however, their activity is dependent on specific sequence composition. This study aims to enhance peptide activity using a module substitution strategy.
Qingping, Liang   +9 more
openaire   +2 more sources

Revisiting the mechanisms of ACE inhibitory peptides from food proteins

Trends in Food Science & Technology, 2017
Abstract Background Angiotensin converting enzyme (ACE) is a key enzyme in the renin angiotensin system (RAS) responsible for conversion of angiotensin (Ang) I into Ang II, a vasoconstrictor leading to elevated blood pressure. ACE inhibitory (ACEi) peptides derived from food proteins have shown potential in the prevention and management of ...
Jianping Wu   +2 more
openaire   +1 more source

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