PERSPECTIVES OF BIOINFORMATICS FOR RESEARCHING FOOD BIOACTIVE PEPTIDES USING IN SILICO INSTRUMENTS

Author(s):  
К.А. РЯЗАНЦЕВА ◽  
Е.Ю. АГАРКОВА

В статье приведен обзор основных классических подходов к производству биологически активных пептидов (БП) и способы их идентификации. Показано, что традиционно используемые способы получения и анализа БП требуют значительных временных и материальных затрат, что ограничивает подробные исследования и оперативную разработку БП. Новые биоинформационные подходы in silico, используемые для идентификации, характеристики, разработки биоактивных механизмов и производства БП из пищевых белков, могут упростить получение и исследование БП, что позволит ускорить разработку функциональных продуктов с использованием БП. The article describes the main classical approaches to the production of biologically active peptides and methods for their identification. It has been shown that the traditionally used methods of obtaining and analyzing bioactive peptides (BP) are not only very costly, but also require a significant amount of time, which limits detailed research and rapid development of BP. New bioinformatic approaches in silico used for identification, characterization, development of bioactive mechanisms and production of BP from food proteins can simplify the production and study of biologically active peptides, which will speed up the development of functional products using BP.

Author(s):  
Małgorzata Darewicz ◽  
Justyna Borawska ◽  
Piotr Mińkiewicz ◽  
Anna Iwaniak ◽  
Piotr Starowicz

2018 ◽  
Vol 88 (5-6) ◽  
pp. 319-343 ◽  
Author(s):  
Elham Nourmohammadi ◽  
Alireza Sadeghi Mahoonak

Abstract. Today, due to immobility, improper food habits, and changes in lifestyle, communities are faced with an increase in health problems such as blood pressure, cholesterol, diabetes, and thrombosis. Bioactive peptides are considered as being the main products of protein hydrolysis which exert high effects on the nervous, immune, and gastrointestinal systems. Unlike synthetic drugs, bioactive peptides have no side effects and this advantage has qualified them as an alternative to such drugs. Due to the above-mentioned properties, this paper focuses on the study of health-improving attributes of bioactive peptides such as anti-oxidative, anti-hypertensive, immunomodulatory, anti-microbial, anti-allergenic, opioid, anti-thrombotic, mineral-binding, anti-inflammatory, hypocholesterolemic, and anti-cancer effects. We also discuss the formation of bioactive peptides during fermentation, the main restrictions on the use of bioactive peptides and their applications in the field of functional foods. In general, food-derived biologically active peptides play an important role in human health and may be used in the development of novel foods with certain health claims.


2020 ◽  
Vol 16 (12) ◽  
pp. 1687-1718
Author(s):  
Huiwen Hou ◽  
Juan Wang ◽  
Jie Wang ◽  
Wen Tang ◽  
Abdul Sami Shaikh ◽  
...  

In recent years, the development and applications of protein drugs have attracted extensive attention from researchers. However, the shortcomings of protein drugs also limit their further development. Therefore, bioactive peptides isolated or simulated from protein polymers have broad application prospects in food, medicine, biotechnology, and other industries. Such peptides have a molecular weight distribution between 180 and 1000 Da. As a small molecule substance, bioactive peptide is usually degraded by various enzymes in the organism and have a short half-life. At the same time, such substances have poor stability and are difficult to produce and store. Therefore, these active peptides may be modified through phosphorylation, glycosylation, and acylation. Compared with other protein drugs, the modified active peptides are more easily absorbed by the body, have longer half-life, stronger targeting, and fewer side effects in addition to higher bioavailability. In the light of their functions, bioactive peptide can be divided into antimicrobial, anti-tumour, anti-angiogenic, antioxidant, anti-fatigue, and anti-hypertensive peptides. This article mainly focuses on the introduction of several promising biologically active peptides functioning as antimicrobial, anti-tumour, antiangiogenic, and antioxidant peptides from the three aspects modification, structural characteristics and mechanism of action.


Foods ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. 846 ◽  
Author(s):  
Anna Jakubczyk ◽  
Monika Karaś ◽  
Kamila Rybczyńska-Tkaczyk ◽  
Ewelina Zielińska ◽  
Damian Zieliński

Generally, bioactive peptides are natural compounds of food or part of protein that are inactive in the precursor molecule. However, they may be active after hydrolysis and can be transported to the active site. Biologically active peptides can also be synthesized chemically and characterized. Peptides have many properties, including antihypertensive, antioxidant, antimicrobial, anticoagulant, and chelating effects. They are also responsible for the taste of food or for the inhibition of enzymes involved in the development of diseases. The scientific literature has described many peptides with bioactive properties obtained from different sources. Information about the structure, origin, and properties of peptides can also be found in many databases. This review will describe peptides inhibiting the development of current diseases, peptides with antimicrobial properties, and new alternative sources of peptides based on the current knowledge and documentation of their bioactivity. All these issues are part of modern research on peptides and their use in current health or technological problems in food production.


2021 ◽  
pp. 482-494
Author(s):  
Kento Imai ◽  
Dawei Ji ◽  
Ifeanyi D. Nwachukwu ◽  
Dominic Agyei ◽  
Chibuike C. Udenigwe

2009 ◽  
Vol 15 (2) ◽  
pp. 179-191 ◽  
Author(s):  
A. Iwaniak ◽  
J. Dziuba

In silico methods are useful tool in protein structure-functional relationships analysis. BIOPEP and InterPro databases were applied to analyze the presence of bioactive fragments in the domains occurring in the sequences representing the major groups of proteins. Domains found in the proteins analyzed had mostly transporting (bovine β-lactoglobulin), immunoglobulin-like (chicken connectin), alpha-amylase inhibitor (a/β-wheat gliadin), calcium binding (chicken myosin) functions, or allowed straightly to assign the protein to an appropriate superfamily (bovine casein). It confirmed the thesis about the existence of the functional relations between the structure (sequence) and the domains with identified conformation. Amongst the domains present in the protein sequences we revealed the presence of fragments with the activities: antihypertensive, opioid, dipeptidylpeptidase IV inhibitors, immunomodulating, and neuropeptides. In the chicken connectin within the immunoglobulin-like domain we found immunomodulating fragments. InterPro analysis did not reveal the existence of any domains in a soybean globulin. It can be explained by the lack of the key structure information helpful in the defining the structure-function relationships. As the number of information in the applied databases will continue to increase we can expect to find stronger relationships between bioactivity of fragments encrypted in proteins and the functionality of domains. This might allow in the future to find evolutionary similarity between different origin food proteins - sources of bioactive peptides.


2018 ◽  
Vol 293 (21) ◽  
pp. 7907-7915 ◽  
Author(s):  
Rajko Igić

This paper provides a brief historical sketch of the science of biologically active peptides. It also offers the story of how Ervin G. Erdös, a pioneer in the study of metabolism of various peptides, influenced me through collaborations that span many years. I worked in Dr. Erdös's research laboratories in Oklahoma City, Dallas, and Chicago, and we shared research interests through visits across the Atlantic between the former Yugoslavia and the United States. Among other findings, we discovered angiotensin-converting enzyme in the retina, which opened up a new research direction for many scientists interested in serious ocular diseases. This tribute to my mentor paints a portrait of a man who, in addition to his dedication to science and his seminal discoveries about the metabolism of peptides, took the time to invest in training many young scientists. His fine personal qualities explain why all of those who worked with him hold him in such high regard.


2020 ◽  
Vol 5 (2) ◽  
pp. 12-19
Author(s):  
I. M. Chernukha ◽  
N. G. Mashentseva ◽  
D. A. Afanasev ◽  
N. L. Vostrikova

Biologically active peptides (BAP) are regarded as the main products of protein hydrolysis. BAP activity depends on the amino acid sequence molecular weight and chain length, type and charge of an amino acid at the N-terminus and C-terminus, hydrophobic and hydrophilic properties, spatial structure. They positively influence many systems of the human body, including the blood circulatory, nervous, immune, gastrointestinal and other systems. The health-improving effect of bioactive peptides is formed due to their antioxidant, antihypertensive, antithrombotic, immunomodulatory, antimicrobial, anti-allergic, opioid, anti-inflammatory, hypocholesterolemic and anticancer properties. Angiotensin-I-converting enzyme (ACE) inhibitory peptides are most studied due to their effect on blood pressure regulation. Unlike synthetic preparations, biologically active peptides do not have side effects and, therefore, can be used as their alternative. There is a growing commercial interest in peptides generated from meat proteins is in the context of health saving functional foods. The paper describes prospects, pros and cons of using bioactive peptides as functional food ingredients and biologically active food additives.


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