scholarly journals An exploration of bioactive peptides: My collaboration with Ervin G. Erdös

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.

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.


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.


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.


2008 ◽  
Vol 91 (4) ◽  
pp. 981-994 ◽  
Author(s):  
María del Mar Contreras ◽  
Iván López-Expósito ◽  
Blanca Hernández-Ledesma ◽  
Mercedes Ramos ◽  
Isidra Recio

Abstract Biologically active peptides are of particular interest in food science and nutrition because they have been shown to play different physiological roles, including antihypertensive, opioid, antimicrobial, and immunostimulating activities. Because these peptides are generated by protein hydrolysis or fermentation, they can represent only minor constituents in a highly complex matrix and therefore, identification of biologically active peptides in food matrixes is a challenging task in food technology. In this context, mass spectrometry (MS) has developed into a necessary tool to assess quality and safety of food and, more recently, to determine the presence and behavior of functional components such as these bioactive peptides. This review highlights the existing methods based on MS to identify, characterize, and quantify food-derived biologically active peptides, taking into account the different ionization sources used for the analysis of these high-value food components. The quantitative determination of bioactive peptides in food products or biological fluids is also discussed.


2019 ◽  
Vol 2 ◽  
pp. 33-39 ◽  
Author(s):  
Volodymyr Yukalo ◽  
Kateryna Datsyshyn ◽  
Liudmyla Storozh

Milk whey proteins carry out a number of important biological functions and also they are precursors of many biologically active peptides (antihypertensive peptides, antagonists of opioid receptors, regulators of intestinal motility, immunomodulatory, anti-microbial and anti-cancer peptides, appetite regulators and so on.). An important stage in natural bioactive peptides obtaining from milk whey proteins is the isolation of homogeneous proteins-precursors. Considering the significant difference in the molecular masses of whey proteins, a promising method for their selection is gel filtration. The purpose of the research was the fractionation of bioactive peptides precursors from milk whey using gel filtration on Sephadex G-150. The whey was obtained from fresh skimmed milk after isoelectric precipitation of casein. Gel filtration was carried out on the columns from a liquid chromatography kit by the “Reanal” company. The fractional composition and the degree of homogeneity of milk whey proteins were determined by disc-electrophoresis in the plates of a polyacrylamide gel. A repeated gel filtration of fractions from the chromatographic peaks, separated into sections, was performed to increase the fractionation efficiency. While choosing a dextran gel for gel filtration of precursors of biologically active peptides from milk whey proteins, we have taken into account the range of their molecular weights (from 10000 to 150000 Da), the ability to form supramolecular structures (β-LG), as well as the previously obtained results of gel filtration. As a result, it was shown that repeated gel filtration of milk whey on Sephadex G-150 allows efficiently fractionate the proteins-precursors of bioactive peptides. The range of peptides and proteins molecular weights that can be fractionated on this Sephadex is from 5000 to 300 000 Da. The usage of repeated gel filtration on Sephadex G-150 with the chromatogram separation into sectors allows to effectively fractionate proteins-precursors of bioactive peptides from milk whey. In particular, homogeneous β-lactoglobulin (degree of homogeneity > 95 %) and partially purified α-lactalbumin, as well as a group of immunoglobulins and a proteose-peptone fraction were obtained.


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