Structural and functional relationship of Cassia obtusifolia trypsin inhibitor to understand its digestive resistance against Pieris rapae

Zhou, Jiayu; Li, Chaolin; Chen, Anqi; Zhu, Jianquan; Zou, Meng; Liao, Hai; Yu, Yamei

doi:10.1016/j.ijbiomac.2020.01.193

Cited by 13 publications

(4 citation statements)

References 51 publications

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“…Studies have shown that the key factor affecting ACE inhibition by peptides is hydrophobic amino acids, and hydrophobic amino acids account for a large proportion of ACE-inhibitory peptides ( 46 ). The main peptide bond of Flavourzyme is related to the carboxyl group of aromatic amino acids ( 47 ); the target peptide bond of Alkaline protease is its carboxyl-terminal hydrophobic amino acid ( 48 ). Therefore, we speculate that Flavourzyme can destroy the protein structure of mulberry leaf protein and completely degrade mulberry leaf protein so that the enzymolysis products are rich in oligopeptides and small molecular polypeptides of less than 1 kDa.…”

Section: Discussionmentioning

confidence: 99%

Preparation and activity evaluation of angiotensin-I converting enzyme inhibitory peptides from protein hydrolysate of mulberry leaf

Chen

et al. 2023

Front. Nutr.

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Angiotensin-I converting enzyme (ACE) inhibitory peptides drew wide attention in the food industry because of their natural reliability, non-toxicity, and safety. However, the characteristics of ACE inhibitory peptides obtained from protein hydrolysate of mulberry leaf prepared by Flavourzyme were still unclear. Based on the single-factor test, the Plackett–Burman test and response surface test were used to determine the key factors affecting the ACE inhibition rate in mulberry leaf protein hydrolysate and the optimum conditions of enzymatic hydrolysis. The results showed that the optimum technical parameters were as follows: the ratio of material to liquid is 1: 25 (w / v, g/mL), the Flavourzyme to substrate ratio was 3,000 U/g, the temperature of enzymatic hydrolysis was 50°C, pH was 6.3, and the time of enzymatic hydrolysis was 2.9 h. The ACE inhibitory peptides in the mulberry leaf protein hydrolysates were purified by ultrafiltration and gel filtration, aiming to obtain the highest active component. The 12 peptide sequences were identified by reverse liquid chromatography-mass spectrometry, and then, they were docked to the crystal structure of human angiotensin-I converting enzyme (1O8A), and the interaction mechanisms of 12 peptide sequences and 1O8A were analyzed. The docking results showed that among the 12 peptide sequences, ERFNVE (792.37 Da), TELVLK (351.72 Da), MELVLK (366.72 Da), and FDDKLD (376.67 Da), all had the lowest docking energy, and inhibition constant. The chemosynthetic ERFNVE (IC50: 2.65 mg/mL), TELVLK (IC50: 0.98 mg/mL), MELVLK (IC50:1.90 mg/mL) and FDDKLD (IC50:0.70 mg/mL) demonstrated high ACE-inhibitory activity with competitive inhibition mode. These results indicated that the ACE-inhibiting peptides from mulberry leaf protein hydrolyzed (FHMP) had the potential activities to inhibit ACE and could be used as functional food or drugs to inhibit ACE. This work provides positive support for mining the biological activity of mulberry leaves in the treatment of hypertension.

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Section: Discussionmentioning

confidence: 99%

Preparation and activity evaluation of angiotensin-I converting enzyme inhibitory peptides from protein hydrolysate of mulberry leaf

Chen

et al. 2023

Front. Nutr.

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“…There are previous reports on purification of trypsin inhibitors from the seeds of M. pruriens, P. corylifolia L. sativus and Trigonella foenum graecum respectively, which is in support of our results ( Borde et al, 2012 ; Yang et al, 2006 ; Ramakrishna et al, 2010 and Oddepally et al, 2013 ). Zhou et al (2020) studied the X-ray structure of trypsin inhibitor purified from Cassia obtusifolia and gave inhibitory activity comparable with that of soybean trypsin inhibitor against midgut trypsin from Pieris rapae. Ferreira et al (2019) purified two recombinant PIs namely, cruzipain inhibitor (rBbCI) and kallikrein inhibitor (rBbKI) from Bauhinia bauhinioides and analyzed its insecticidal activity against soldiers and workers of Nasutitermes.…”

Section: Discussionmentioning

confidence: 99%

In vitro screening of peptidase inhibitory activity in some plants of North India

Samiksha

Sohal

2020

Heliyon

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In the present study, trypsin and chymotrypsin inhibitory activity of some plants of different families was evaluated. A total of 55 plants were screened, out of which six showed the maximum trypsin inhibitory activity namely Acacia concinna, Caesalpinia bonducella, Lathyrus sativus, Mucuna pruriens, Psoralea corylifolia and Sapindus mukorossi . Results suggested that the plants showing trypsin inhibitory activity (TIA) also have chymotrypsin inhibitory activity (CIA). Both trypsin and chymotrypsin inhibitory activities were high in seeds compared to leaves followed by flowers. It was also observed that TIA was maximally present in Sapindaceae family whereas CIA was maximum in fabaceae family followed by others.

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“…High structural affinities between the inhibitor and the enzyme. [132] Trypsin inhibitors from tamarind seed (pTTI)…”

Section: In Silico Methods Outcomes Referencesmentioning

confidence: 99%

Host Cell Proteases Mediating SARS-CoV-2 Entry: An Overview

Oubahmane

Hdoufane

Bjij

et al. 2022

CTMC

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The outbreak of the SARS-CoV-2 virus in late 2019 and the spread of the COVID-19 pandemic have caused severe health and socioeconomic damage worldwide. Despite the significant research effort to develop vaccines, antiviral treatments, and repurposed therapeutics to effectively contain the catastrophe, there are no available effective vaccines or antiviral drugs that are able to limit the threat of the disease, so the infections continue to expand. To date, the search for effective treatment remains a global challenge. Therefore, it is imperative to develop therapeutic strategies to contain the spread of SARS-CoV-2. Like other coronaviruses, SARS-CoV-2 invades and infects human host cells via the attachment of its spike envelope glycoprotein to the human host cell receptor hACE2. Subsequently, several host cell proteases facilitate viral entry via proteolytic cleavage and activation of the S protein. These host cell proteases include, type II transmembrane serine proteases (TTSPs), cysteine cathepsins B and L, furin, trypsin, and Factor Xa among others. Given the critical role of the host cell proteases in coronavirus pathogenesis, their inhibition by small molecules has successfully targeted SARS-CoV-2 in vitro, suggesting that host cell proteases are attractive therapeutic targets for SARS-CoV-2 infection. In this review, we focus on the biochemical properties of host cell proteases that facilitate the entry of SARS-CoV-2, and we highlighted therapeutic small molecule candidates that have been proposed through in silico research.

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Structural and functional relationship of Cassia obtusifolia trypsin inhibitor to understand its digestive resistance against Pieris rapae

Cited by 13 publications

References 51 publications

Preparation and activity evaluation of angiotensin-I converting enzyme inhibitory peptides from protein hydrolysate of mulberry leaf

Preparation and activity evaluation of angiotensin-I converting enzyme inhibitory peptides from protein hydrolysate of mulberry leaf

In vitro screening of peptidase inhibitory activity in some plants of North India

Host Cell Proteases Mediating SARS-CoV-2 Entry: An Overview

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