scholarly journals Application of Mass Spectrometry to the Characterization and Quantification of Food-Derived Bioactive Peptides

2008 ◽  
Vol 91 (4) ◽  
pp. 981-994 ◽  
Author(s):  
María del Mar Contreras ◽  
Iván López-Expósito ◽  
Blanca Hernández-Ledesma ◽  
Mercedes Ramos ◽  
Isidra Recio
Keyword(s):  
Mass Spectrometry ◽  
Bioactive Peptides ◽  
Biological Fluids ◽  
Biologically Active ◽  
Active Peptides ◽  
Ionization Sources ◽  
Biologically Active Peptides ◽  
Assess Quality ◽  
And Behavior ◽  
Functional Components

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.

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

2020 ◽  
Author(s):  
К.А. РЯЗАНЦЕВА ◽  
Е.Ю. АГАРКОВА
Keyword(s):  
In Silico ◽  
Bioactive Peptides ◽  
Rapid Development ◽  
Biologically Active ◽  
Food Proteins ◽  
Active Peptides ◽  
Biologically Active Peptides ◽  
Speed Up ◽  
Bioinformatic Approaches

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.

Health Implications of Bioactive Peptides: A Review

2018 ◽  
Vol 88 (5-6) ◽  
pp. 319-343 ◽  
Author(s):  
Elham Nourmohammadi ◽  
Alireza Sadeghi Mahoonak
Keyword(s):  
Food Habits ◽  
Bioactive Peptides ◽  
Biologically Active ◽  
Health Claims ◽  
Novel Foods ◽  
Active Peptides ◽  
Synthetic Drugs ◽  
Anti Cancer ◽  
Biologically Active Peptides ◽  
Mineral Binding

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.

A Review of Bioactive Peptides: Chemical Modification, Structural Characterization and Therapeutic Applications

2020 ◽  
Vol 16 (12) ◽  
pp. 1687-1718
Author(s):  
Huiwen Hou ◽  
Juan Wang ◽  
Jie Wang ◽  
Wen Tang ◽  
Abdul Sami Shaikh ◽  
...  
Keyword(s):  
Half Life ◽  
Bioactive Peptides ◽  
Structural Characteristics ◽  
The Body ◽  
Biologically Active ◽  
Bioactive Peptide ◽  
Protein Drugs ◽  
Active Peptides ◽  
Biologically Active Peptides ◽  
Further Development

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.

scholarly journals Current Trends of Bioactive Peptides—New Sources and Therapeutic Effect

Foods ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. 846 ◽  
Author(s):  
Anna Jakubczyk ◽  
Monika Karaś ◽  
Kamila Rybczyńska-Tkaczyk ◽  
Ewelina Zielińska ◽  
Damian Zieliński
Keyword(s):  
Bioactive Peptides ◽  
Current Knowledge ◽  
Antimicrobial Properties ◽  
Biologically Active ◽  
Active Peptides ◽  
Current Trends ◽  
Bioactive Properties ◽  
Biologically Active Peptides ◽  
Alternative Sources ◽  
Different Sources

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.

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

2018 ◽  
Vol 293 (21) ◽  
pp. 7907-7915 ◽  
Author(s):  
Rajko Igić
Keyword(s):  
Bioactive Peptides ◽  
Research Direction ◽  
The United States ◽  
Biologically Active ◽  
Active Peptides ◽  
Biologically Active Peptides ◽  
High Regard ◽  
Personal Qualities ◽  
New Research ◽  
Historical Sketch

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.

scholarly journals Biochemical and biophysical investigation of the HalM2 lanthipeptide synthetase using mass spectrometry

2021 ◽  
Author(s):  
Sally R. Hamry ◽  
Christopher James Thibodeaux
Keyword(s):  
Mass Spectrometry ◽  
Biologically Active ◽  
Clinical Settings ◽  
Molecular Scaffold ◽  
Active Peptides ◽  
Large Size ◽  
Biologically Active Peptides ◽  
Dynamic Structures ◽  
Modified Forms ◽  
Rapid Emergence

The rapid emergence of antimicrobial resistance in clinical settings has called for renewed efforts to discover and develop new antimicrobial compounds. Lanthipeptides present a promising, genetically-encoded molecular scaffold for the engineering of structurally complex, biologically active peptides. These peptide natural products are constructed by enzymes (lanthipeptide synthetases) with relaxed substrate specificity that iteratively modify the precursor lanthipeptide to generate structures with defined sets of thioether macrocycles. The mechanistic features that guide the maturation of lanthipeptides into their proper, fully-modified forms are obscured by the complexity of the multistep maturation, and the large size and dynamic structures of the synthetases and precursor peptides. Over the past several years, our lab has been developing a suite of mass spectrometry-based techniques that are ideally suited to untangling the complex reaction sequences and molecular interactions that define lanthipeptide biosynthesis. This review focuses on our development and application of these MS-based techniques to investigate the biochemical, kinetic, and biophysical properties of the haloduracin  class II lanthipeptide synthetase, HalM2.

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