Antioxidant and Cholinesterase Inhibitory Activity of a New Peptide From <i>Ziziphus jujuba</i> Fruits

Zare‐Zardini, Hadi; Tolueinia, Behnaz; Hashemi, A; Ebrahimi, Leila; Fesahat, Farzaneh

doi:10.1177/1533317513500839

Cited by 63 publications

(32 citation statements)

References 51 publications

(55 reference statements)

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“…Therefore, recent efforts have focused on the development of natural AChE‐inhibitory alternatives, such as plant secondary metabolites, which have been mainly polyphenolic compounds (Akomolafe, ; Ghribia et al, ; Iannello et al, ; Kumar & Chowdhury, ; Odubanjo, Oboh, Oyeleye, & Adefegha, ). However, in addition to the polyphenols, isolation of a polypeptide that showed strong in vitro AChE‐inhibitory activity has been reported (Zare‐Zardini et al, ).…”

Section: Introductionmentioning

confidence: 99%

“…This abberant brain and neurotransmission condition leads to Alzheimer's disease (AD) pathogenesis (Li et al, 2015;Willcox, Scapagnini, & Willcox, 2014) that contributes to increased global morbidity/mortality rate (US Burden of Disease Collaborators, 2013). The high catalytic efficiency (CE) of AChE and the importance of its inhibition in AD management has been an important research focus in the development of various therapeutic agents (Acharya, Dutta, Chaudhury, & De, 2018;Li et al, 2015;Olarewaju et al, 2018;Saravanaraman, Chinnadurai, & Boopathy, 2014;Taslimi & Gulçin, 2018;Yadav & Appukuttan, 2019;Yatesa et al, 2019;Zare-Zardini, Tolueinia, Hashemi, Ebrahimi, & Fesahat, 2013). Several synthetic AChE-inhibitory drugs have been developed for use against neurodegenerative diseases, such as dementia and AD; however, these drugs are associated with severe negative side effects (Ghribia, Ghouilaa, Omrib, Besbesb, & Janneta, 2014;Iannello et al, 2014;Kumar & Chowdhury, 2014).…”

Section: Introductionmentioning

confidence: 99%

“…However, in addition to the polyphenols, isolation of a polypeptide that showed strong in vitro AChE-inhibitory activity has been reported (Zare-Zardini et al, 2013).…”

Section: Introductionmentioning

confidence: 99%

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Kinetics of acetylcholinesterase inhibition by hemp seed protein‐derived peptides

Malomo

Aluko

2019

J Food Biochem

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The aim of this work was to enhance the acetylcholinesterase (AChE)‐inhibitory activity of a pepsin‐produced hemp seed protein hydrolysates (HPH) through reverse‐phase HPLC separation followed by identification of peptide sequences present in the most active fraction. The HPH was separated into eight fractions (F1–F8) with F7 exhibiting significantly (p < 0.05) the strongest (97.5%) in vitro inhibition of electric eel AChE (eeAChE) activity in comparison to 53.8% for HPH. The HPH consisted mostly of low molecular weight peptides of < 11 amino acid residues and most contained at least one hydrophobic amino acid. Kinetics of enzyme inhibition revealed a mixed‐type inhibition of eeAChE activity by HPH whereas F7 acted through an uncompetitive mode; in contrast inhibition of human AChE by HPH and F7 was uncompetitive. The stronger inhibitory potency of the F7 peptides fraction against both enzymes was confirmed through reduced maximal velocity, catalytic efficiency, and inhibition constant values when compared to the HPH. Practical applications The use of natural products for the prevention or treatment of human diseases continues to be an area of intense research activities. Food protein‐derived peptides obtained through enzymatic hydrolysis of hemp seed proteins were shown in vitro to be strong inhibitors of activities of both the eel and human forms of acetylcholinesterase (AChE). AChE is an important therapeutic target because excessive activity of this enzyme is a causative factor of neurodegenerative diseases such as dementia and Alzheimer's. This work showed that peptides in the most active fraction are small in sizes, which may favor their absorption into blood circulation and possible permeation of the blood–brain barrier. Therefore, the hemp seed peptides are potential agents that can be used to formulate functional foods and nutraceuticals against neurodegenerative diseases.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Kinetics of acetylcholinesterase inhibition by hemp seed protein‐derived peptides

Malomo

Aluko

2019

J Food Biochem

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“…Therefore, due to the scarce information in literature, comparison of the inhibitory activity against AChE of the different peptide or glycopeptide fractions of the mannoprotein hydrolysates obtained in this study is a difficult task. One of such peptides with anti-AChE activity that has been found and characterized is the cationic peptide Snakin-Z, isolated from fruits of Zizyphus jujuba, a medicinal plant [29]. This peptide has a molecular mass of 3318.82 Da and the following sequence: CARLNCVPKGTSGNTETCPCYASLHSCRKYG.…”

Section: Chromatographic Separation Of the Most Active Fractions Agaimentioning

confidence: 99%

Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins

Pablo¹

2018

IJMB

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Purified mannoproteins from 5 yeast strains belonging to the genera Brettanomyces, Candida, Pichia and Saccharomyces were studied. Each mannoprotein extract was hydrolysed with proteolytic enzymes, generating small peptides whose inhibitory activity against acetylcholinesterase (AChE) was determined. Partial purification of six selected mannoprotein extracts was done by reversed phase chromatography, six fractions with relevant inhibitory activity being obtained. Chromatographic and spectroscopic analyses revealed mainly hydrophilic peptides, with molecular weight between 700 and 4800 Da. The presence of sugars in all fractions was determined, mannose being the most abundant one. Subsequently, the most active fractions were again separated by affinity chromatography, which led to two new types of fractions: peptidic fractions (PFs) and glycopeptidic fractions (GPFs). Results showed that all fractions inhibited AChE, although GPFs inhibited AChE to a greater degree than PFs, with a percentage of inhibition ranging from 49.3 to 77.8%. Likewise, all GPFs fractions had higher values of inhibition than the corresponding whole fraction, while PFs showed lower percentages of antiacetylcholinesterase activity. These results suggest that glycopeptidic are the most interesting fractions for their ability to inhibit this enzyme. As a conclusion, it was shown that some peptides produced by hydrolysis of mannoproteins proved able to inhibit AChE and should be considered as potential anti-AChE agents and significant to the manufacturing of food with potential functional properties.

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“…The main actions of these peptides are disruption of the structure or function of microbial cell membranes and are synthesized in response to infection or inflammation (3,4). These agents have different useful other biological activities so that there is possibility to develop and introduce them as new drugs for treatment and prevention of various diseases (5)(6)(7)(8)(9).…”

Section: Introductionmentioning

confidence: 99%

Hemocompatibility Evaluation of Two Antimicrobial Peptides, Plantaricin CS and Snakin Z

Zare‐Zardini¹,

Rezaei²,

Arab-Badkubeh³

et al. 2016

West Indian Med J

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Objective: Plantaricin CS and Snakin Z are two peptides that purified from innate immune systems of two different species. Because of their biological activities, the use of these peptides in a variety of medical applications is possible. For this purposes, investigation of hemocompatibility and cytotoxicity of peptides is necessary. Methods: Human red blood cells (RBCs) were treated with different concentration of peptide in two methods: radial diffusion assay and spectrophotometric assay. For in vivo assay, the mean of hematocrit, RBCs and White Blood Cells (WBCs) was assessed after treatment of 48 rats (24 rats for each peptide) with different concentrations of peptides (5,15,45,135 and 400µg/ml) for two weeks. Results: According to data, no significant changes were observed in the groups treated with Plantaricin CS in all concentration; but Snakin Z showed significant toxicity on all blood cells. This peptide decreases the RBC, WBC and Hematocrit as 4.1 RBC×1000000/µL, 12 WBC×1000/µL and 16% in concentration of 400 µg/ml, respectively. Conclusion: According to this study, both of peptides showed hemocompatibility in values that they have biological activities. So it's suggested that Snakin Z and Plantaricin CS may be suitable pharmaceutical agents.

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Antioxidant and Cholinesterase Inhibitory Activity of a New Peptide From Ziziphus jujuba Fruits

Cited by 63 publications

References 51 publications

Kinetics of acetylcholinesterase inhibition by hemp seed protein‐derived peptides

Kinetics of acetylcholinesterase inhibition by hemp seed protein‐derived peptides

Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins

Hemocompatibility Evaluation of Two Antimicrobial Peptides, Plantaricin CS and Snakin Z

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