FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2325138819> ?p ?o ?g. }

• W2325138819 abstract "Immunomodulatory peptides play an important role in immune response. Researchers acquired activity peptides from natural food protein by enzymatic hydrolysis and the most commonly used enzymes are Alcalase. In this paper, the mechanism of immunomodulation was summarized briefly. The peptides charge, hydrophobicity and the length of peptide chain have great influences on the immunomodulating activities of peptides. Introduction It has been reported that more than 1500 different bioactive peptides were found and more than 1250 peptides with different functional significances [1], immunomodulatory peptides was one of them. These bioactive peptides could be used for anti-oxidative, antifungal, antithrombotic, sensory physiological activities and can enhance the nutritional value of food [2]. Immunomodulatory peptides modulate [3] the immune response through improving the antibody production of secretory lgA and epithelial barrier function, modulating apoptosis and TLR4 binding, inducing regulatory T cells and B cells, and controlling cytokine production. The immunomodulatory peptides generated from natural sources usually have varieties of functions but not only for immunomodulatory. Peptide fraction from the larvae of Musca domestica not only has the ability of immunomodulatory, but also plays an important role in anti-tumor [4]. Dipeptidyl peptidase 4 inhibitors could stimulate the immune system 1 and 2 and also be used in the treatment of type 2 diabetes mellitus [5]. It has reveal immunomodulatory peptides not only for immunoregulation, but also could be used for other fields. Preparation of immunomodulatory peptides Enzymatic hydrolysis. Since Jolles acquired a sort of immunomodulatory peptides from milk protein by trypsin for the first time [6], a growing number of people have paid attention to generate peptides from natural sources such as milk, grain and shark meat. It was focused on the use of by-products of food protein bio-processing for immunomodulatory peptides which could enhance the production value and reduce the cost of waste disposal [7]. Immunomodulatory peptides show no activity when contained with the whole protein sequence, but can be released by enzymatic proteolysis. The enzymes used for hydrolysis could be divided into digestive system or microbial origin [8]. Microbial fermentation and food processing could also be used for producing immunomodulatory peptides separated from enzymatic proteolysis. As shown in Table 1, several enzymes had been successfully applied to hydrolysis kinds of natural protein sources to acquire bioactive peptides like whey protein, soy protein, corn protein, oyster protein. It can be found that from these data, the most common enzymes are Alcalase, trypsin and pepsin. The immunomodulatory peptides generated by enzymatic hydrolysis in vitro probably be absorbed more effectively than released from dietary proteins during the digestive process in the gut [9]. In recent years, food-hydrolyzed peptides enriched were added to immunomodulatory diets, like wheyhydrolyzed peptides enriched used to prevent fibrosis. 4th International Conference on Machinery, Materials and Computing Technology (ICMMCT 2016) © 2016. The authors Published by Atlantis Press 1480 Table 1 Immunomodulatory peptides derived from sources Source of peptides Conditions Indicator References enzymes pH T/ °C Time/min Labeorohita roe Pepsin 2 37 120 ABCDEF [10] Trypsin 8 37 150 Alcalase 8 55 180 Alaska pollock frame protein Trypsin 8 20 290 A [11] Whey protein Alcalase 8 50 A [12] Soy proteins Alcalase 8 60 225 AB [13] Oysters protein Protease 7.5 50 300 ABC [14] Corn protein Alkaline 8.5 55 180 G [15] Neutral 7 45 120 Green microalga Pancreatin 7.5 45 240 B [16] A-splenic lymphocyte proliferation, B-phagocytosis capacity of peritoneal macrophages, C-natural killer (NK) cell activity, D-splenic T lymphocyte, E-small intestine mucosal immunity (secretory-IgA), F-serum immunoglobulins (IgA, IgM & IgG), G-antihypertensive activity. Separation and purification. It has been reported that the molecular weight of most immunomodulatory peptides were less than 2 kDa, so the separation and purification of immunomodulatory peptides play an important role in analyzing immunomodulatory peptides activity. Milda obtained peptides of less than 3 kDa with significantly decreased the basal nuclear factor (NF)-κB activity in Caco-2 cells through Ultracel regenerated cellulose ultrafiltration membrane [17]. Chromatographic separation, especially high-performance liquid chromatography (HPLC), and gel electrophoresis were also widely used in the separation and purification of immunomodulatory peptides, but the HPLC was more effective than gel electrophoresis when be used in industry because of different throughput and costing. The mechanism of immunomodulation It is well-known that the composition of amino acid, sequence and special structure influences the immunomodulation of protein peptides. So the factors influenced immunomodulatory activities have aroused increasing interests among researchers. Bioactive peptides were composed of 3 to 20 amino acids and have a positive impact on human health. As show in Table 2, immunomodulatory peptides are usually consist of hydrophobic amino acid, such as Ala, Val, Met, Ple, Ile, Leu, Pro, Trp, is in agreement with report of Easton. However, it has been postulated that overall ability of immunomodulatory must be attributed to comprehensive effects of a lot of factors rather than to the individual effect of the hydrophobicity of amino acid. Three structurally related small molecular weight peptides with limited sequence similarity to frenatin were compared and demonstrated to the C-terminal α-amidation, which plays an important role in immunoregulation [18]. It also has been observed that lower molecular weight and positively charged peptides plays the key role when it stimulated lymphocyte proliferation at much lower concentration [19]." @default.
• W2325138819 created "2016-06-24" @default.
• W2325138819 creator A5009310956 @default.
• W2325138819 creator A5044712592 @default.
• W2325138819 creator A5091157375 @default.
• W2325138819 date "2016-01-01" @default.
• W2325138819 modified "2023-09-25" @default.
• W2325138819 title "The Research Progress of Immunomodulatory Peptides" @default.
• W2325138819 cites W113690590 @default.
• W2325138819 cites W1542076407 @default.
• W2325138819 cites W1972746206 @default.
• W2325138819 cites W1976674685 @default.
• W2325138819 cites W1982498757 @default.
• W2325138819 cites W1985086212 @default.
• W2325138819 cites W1988166376 @default.
• W2325138819 cites W1988390813 @default.
• W2325138819 cites W1996079780 @default.
• W2325138819 cites W2007581219 @default.
• W2325138819 cites W2007628916 @default.
• W2325138819 cites W2009173591 @default.
• W2325138819 cites W2014755465 @default.
• W2325138819 cites W2028434828 @default.
• W2325138819 cites W2033982089 @default.
• W2325138819 cites W2045599308 @default.
• W2325138819 cites W2050150310 @default.
• W2325138819 cites W2071055024 @default.
• W2325138819 cites W2077401288 @default.
• W2325138819 cites W2137988269 @default.
• W2325138819 cites W2163522651 @default.
• W2325138819 doi "https://doi.org/10.2991/icmmct-16.2016.294" @default.
• W2325138819 hasPublicationYear "2016" @default.
• W2325138819 type Work @default.
• W2325138819 sameAs 2325138819 @default.
• W2325138819 citedByCount "0" @default.
• W2325138819 crossrefType "proceedings-article" @default.
• W2325138819 hasAuthorship W2325138819A5009310956 @default.
• W2325138819 hasAuthorship W2325138819A5044712592 @default.
• W2325138819 hasAuthorship W2325138819A5091157375 @default.
• W2325138819 hasBestOaLocation W23251388191 @default.
• W2325138819 hasConcept C170493617 @default.
• W2325138819 hasConcept C181199279 @default.
• W2325138819 hasConcept C185592680 @default.
• W2325138819 hasConcept C203014093 @default.
• W2325138819 hasConcept C2779281246 @default.
• W2325138819 hasConcept C2781063702 @default.
• W2325138819 hasConcept C2781307694 @default.
• W2325138819 hasConcept C2781469919 @default.
• W2325138819 hasConcept C55493867 @default.
• W2325138819 hasConcept C86803240 @default.
• W2325138819 hasConcept C88016717 @default.
• W2325138819 hasConcept C8891405 @default.
• W2325138819 hasConceptScore W2325138819C170493617 @default.
• W2325138819 hasConceptScore W2325138819C181199279 @default.
• W2325138819 hasConceptScore W2325138819C185592680 @default.
• W2325138819 hasConceptScore W2325138819C203014093 @default.
• W2325138819 hasConceptScore W2325138819C2779281246 @default.
• W2325138819 hasConceptScore W2325138819C2781063702 @default.
• W2325138819 hasConceptScore W2325138819C2781307694 @default.
• W2325138819 hasConceptScore W2325138819C2781469919 @default.
• W2325138819 hasConceptScore W2325138819C55493867 @default.
• W2325138819 hasConceptScore W2325138819C86803240 @default.
• W2325138819 hasConceptScore W2325138819C88016717 @default.
• W2325138819 hasConceptScore W2325138819C8891405 @default.
• W2325138819 hasLocation W23251388191 @default.
• W2325138819 hasOpenAccess W2325138819 @default.
• W2325138819 hasPrimaryLocation W23251388191 @default.
• W2325138819 hasRelatedWork W1486012885 @default.
• W2325138819 hasRelatedWork W1596159869 @default.
• W2325138819 hasRelatedWork W181640332 @default.
• W2325138819 hasRelatedWork W2058685922 @default.
• W2325138819 hasRelatedWork W2123715695 @default.
• W2325138819 hasRelatedWork W2364156843 @default.
• W2325138819 hasRelatedWork W2373912901 @default.
• W2325138819 hasRelatedWork W2434060905 @default.
• W2325138819 hasRelatedWork W2588794403 @default.
• W2325138819 hasRelatedWork W2912698279 @default.
• W2325138819 hasRelatedWork W2950991123 @default.
• W2325138819 hasRelatedWork W2956732111 @default.
• W2325138819 hasRelatedWork W3011245543 @default.
• W2325138819 hasRelatedWork W3039955071 @default.
• W2325138819 hasRelatedWork W3045686118 @default.
• W2325138819 hasRelatedWork W3194765430 @default.
• W2325138819 hasRelatedWork W1506516392 @default.
• W2325138819 hasRelatedWork W2266274937 @default.
• W2325138819 hasRelatedWork W2283060587 @default.
• W2325138819 hasRelatedWork W2967305253 @default.
• W2325138819 isParatext "false" @default.
• W2325138819 isRetracted "false" @default.
• W2325138819 magId "2325138819" @default.
• W2325138819 workType "article" @default.