QSAR-aided in silico approach in evaluation of food proteins as precursors of ACE inhibitory peptides

Gu, Yuchen; Majumder, Kaustav; Wu, Jianping

doi:10.1016/j.foodres.2011.01.051

Cited by 115 publications

(53 citation statements)

References 48 publications

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“…85 The ACE IC 50 value of peptides predicted in silico to be released from the major proteins present in 15 food commodities by thermolysin and combinations of thermolysin and pepsin then thermolysin, pepsin and trypsin were determined by QSAR. This analysis allowed the identication of meat (pork, beef and chicken) proteins as rich sources for potent ACE inhibitory peptides (IC 50 < 10 mM).…”

Section: Limitations Of Qsar For the Study Of Bapsmentioning

confidence: 99%

Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review

Nongonierma

Fitzgerald

2016

RSC Adv.

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Section: Limitations Of Qsar For the Study Of Bapsmentioning

confidence: 99%

Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review

Nongonierma

Fitzgerald

2016

RSC Adv.

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“…These peptides, in addition to inhibiting the activity of ACE in vitro (IC 50 <10µM) after hydrolysis by thermolysine, also resisted the action of pepsin and trypsin, remaining intact and active, which highly increases the probability they are absorbed and exercise in the general metabolism the antihypertensive functions. The results obtained by Gu et al, [19] indicated that the proteins of meat (pigs, cattle, and poultry) released the highest number of active peptides (IC 50 <10µM), followed by the proteins of milk, egg, soybean, and canola, while the proteins of fish (except for salmon) and cereals (except for oats and barley) contain the lowest number of peptides of high activity. A high number of these peptides remained active after being subjected to the action of pepsin and trypsin.…”

Section: Antihypertensive Peptidesmentioning

confidence: 97%

“…In a recent work, Gu et al, [19] systematically researched the potential of the main food proteins as precursors of ACE inhibitory peptides, with the aid of the QSAR in silico technique in order to establish the rationality of choice of more appropriate proteins as substrate in the preparation of these peptides. The in silico digestion of proteins present in 15 foods that are common in the human diet, of vegetable origin (soybeans, peas, barley, oats, canola), milk proteins (αs1 and αs2 caseins, κ-casein, β-lactoferrin, α-lactalbumin), meat (pigs, cattle, poultry), and fish (tuna, salmon, hake) generated, based on the specificity of the proteolytic enzyme thermolysine, 5,709 peptides in the range of 2 to 6 amino acid residues.…”

Section: Antihypertensive Peptidesmentioning

confidence: 99%

“…Two synthetic peptides corresponding to α-LA, Tyr-Gly (f:50-51) and Tyr-Gly-Gly (f: [18][19][20], stimulated protein synthesis and the proliferation of peripheral lymphocytes isolated from human blood, when stimulated by Concanavalin A (Con A), a mitogenic protein.…”

Section: Immunomodulatory Peptidesmentioning

confidence: 99%

“…This strategy is the Quantitative Structure-Activity Relationship (QSAR) analysis, based on prior knowledge of the amino acid sequence in the polypeptide chain and of the specificity of a certain number of proteolytic enzymes tested. Based on these two parameters, computer programs (software) are established that are capable of predicting the number of peptides released by specific proteases with potential to exercise different bioactivities, a methodology now known as proteolysis or digestibility in silico [19]. However, a detailed experimental work should be conducted with the peptide identified and isolated to confirm possible bioactivities and repeatability as well as the feasibility of the process in silico.…”

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confidence: 99%

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Food Proteins and Bioactive Peptides, Functional Diets

Sgarbieri¹,

Armadas²

2017

FSN

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Throughout the second half of the last century and early this century the concept of the biological function of food proteins has changed significantly. While in the past the food proteins were regarded only as macronutrients capable of providing the amino acids to form the protein component of organs and tissues, also participating in the generation of metabolic energy for the normal functioning of living organisms, today it is known that certain proteins present in food, as well as fragments or peptides derived thereof, may participate in the general metabolism in a much more interactive manner, through bioactivities that go far beyond the nutritional functions that had been established by the end of the first half of the prior century.By making an analogy with the aeronautical activity we can say that in the past the food proteins functioned as black boxes holding numerous important pieces of information, which research and technology have only revealed, in part, in recent decades. In this period it Received: August 07, 2017; Accepted: September 12, 2017; Published: September 26, 2017 was found that certain proteins present in foods are naturally bioactive, and can be absorbed from the Gastrointestinal System (GIS) in their intact or slightly modified form and exercise specific bioactivities in the systemic metabolism [1], or, in addition, resist the action of digestive enzymes exercising different bioactivities in the gastrointestinal system [2]. Even more interesting were the findings that food proteins, of both plant and animal origin, contain, in their primary structures, specific amino acid sequences in their polypeptide chains, which when cleaved in the form of peptides by proteolytic enzymes or by specific chemical reagents may exercise diverse bioactivities that were latent in the original structure of the protein from which they originated.Bioactive peptides have been obtained from precursor proteins through the use of methodologies that have reached a high degree of sophistication and complexity, such as: (a) enzymatic hydrolysis by digestive enzymes; (b) proteolysis of the protein source by enzymes derived from microorganisms or plants; (c) fermentation process using culture with high proteolytic power and specificity. The bioactive potential of the peptides originating from the proteolysis of food proteins can be explored in the integral hydrolysates, produced in special conditions. However, in the current literature there are numerous research works and literature reviews emphasizing the importance of the isolation, purification, characterization, study of mechanisms and impact of these peptides on human health [3][4][5][6][7][8]. Production and Processing of Bioactive Peptides Derived from Food ProteinsA large number of plants and animals have been object of study as source of Bioactive Peptides (BAPs). Several studies were conducted, particularly with milk proteins [9,10], eggs [11,12], and muscle proteins from pigs [13], cattle [14], poultry [15], and fish [16]. BAPs have been obtained from...

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