LIVIVO - Search results -

Search results

Result 1 - 10 of total 17

Search options

Article ; Online: Ultrasensitive Quantification of Crustacean Tropomyosin by Immuno-PCR.

Radomirović, Mirjana / Gligorijević, Nikola / Stanić-Vučinić, Dragana / Rajković, Andreja / Ćirković Veličković, Tanja

International journal of molecular sciences

2023 Volume 24, Issue 20

Abstract: Tropomyosin is the major and predominant allergen among shellfish. This study developed an ultrasensitive immuno-PCR method for the quantification of crustacean tropomyosin in foods. The method couples sandwich ELISA with the real-time PCR (rtPCR) ... ...

Abstract	Tropomyosin is the major and predominant allergen among shellfish. This study developed an ultrasensitive immuno-PCR method for the quantification of crustacean tropomyosin in foods. The method couples sandwich ELISA with the real-time PCR (rtPCR) amplification of marker DNAs. Monoclonal anti-TPM antibody was the capture antibody, polyclonal rabbit anti-shrimp tropomyosin antibody was the detection antibody, while natural shrimp tropomyosin served as the standard. A double-stranded amino-DNA was covalently conjugated to a secondary anti-rabbit antibody and subsequently amplified and quantified via rtPCR. The quantification sensitivity of immuno-PCR was 20-fold higher than analogous ELISA, with LOQ 19.8 pg/mL. The developed immuno-PCR method is highly specific for the detection of crustacean tropomyosin and is highly precise in a broad concentration range. Tropomyosin recovery in the spiked vegetable soup was 87.7-115.6%. Crustacean tropomyosin was also quantified in commercial food products. The reported immuno-PCR assay is the most sensitive method for the quantification of crustacean tropomyosin and is the first immuno-PCR-based assay for the quantification of food allergen and food protein in general. The described method could be easily adapted for the specific and ultrasensitive immuno-PCR-based detection of traces of any food allergen that is currently being quantified with ELISA, which is of critical importance for people with food allergies.
MeSH term(s)	Humans ; Animals ; Rabbits ; Tropomyosin/genetics ; Crustacea ; Shellfish ; Seafood/analysis ; Allergens ; Food Hypersensitivity/diagnosis
Chemical Substances	Tropomyosin ; Allergens
Language	English
Publishing date	2023-10-21
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms242015410
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Article ; Online: Food Antioxidants and Their Interaction with Human Proteins

Nedić, Olgica / Penezić, Ana / Minić, Simeon / Radomirović, Mirjana / Nikolić, Milan / Ćirković Veličković, Tanja / Gligorijević, Nikola

Antioxidants. 2023 Mar. 27, v. 12, no. 4

2023

Abstract: Common to all biological systems and living organisms are molecular interactions, which may lead to specific physiological events. Most often, a cascade of events occurs, establishing an equilibrium between possibly competing and/or synergistic processes. ...

Abstract	Common to all biological systems and living organisms are molecular interactions, which may lead to specific physiological events. Most often, a cascade of events occurs, establishing an equilibrium between possibly competing and/or synergistic processes. Biochemical pathways that sustain life depend on multiple intrinsic and extrinsic factors contributing to aging and/or diseases. This article deals with food antioxidants and human proteins from the circulation, their interaction, their effect on the structure, properties, and function of antioxidant-bound proteins, and the possible impact of complex formation on antioxidants. An overview of studies examining interactions between individual antioxidant compounds and major blood proteins is presented with findings. Investigating antioxidant/protein interactions at the level of the human organism and determining antioxidant distribution between proteins and involvement in the particular physiological role is a very complex and challenging task. However, by knowing the role of a particular protein in certain pathology or aging, and the effect exerted by a particular antioxidant bound to it, it is possible to recommend specific food intake or resistance to it to improve the condition or slow down the process.
Keywords	antioxidants ; blood ; food intake ; humans
Language	English
Dates of publication	2023-0327
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article ; Online
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox12040815
Database	NAL-Catalogue (AGRICOLA)

Order via subito

Article: Food Antioxidants and Their Interaction with Human Proteins.

Nedić, Olgica / Penezić, Ana / Minić, Simeon / Radomirović, Mirjana / Nikolić, Milan / Ćirković Veličković, Tanja / Gligorijević, Nikola

Antioxidants (Basel, Switzerland)

2023 Volume 12, Issue 4

Abstract	Common to all biological systems and living organisms are molecular interactions, which may lead to specific physiological events. Most often, a cascade of events occurs, establishing an equilibrium between possibly competing and/or synergistic processes. Biochemical pathways that sustain life depend on multiple intrinsic and extrinsic factors contributing to aging and/or diseases. This article deals with food antioxidants and human proteins from the circulation, their interaction, their effect on the structure, properties, and function of antioxidant-bound proteins, and the possible impact of complex formation on antioxidants. An overview of studies examining interactions between individual antioxidant compounds and major blood proteins is presented with findings. Investigating antioxidant/protein interactions at the level of the human organism and determining antioxidant distribution between proteins and involvement in the particular physiological role is a very complex and challenging task. However, by knowing the role of a particular protein in certain pathology or aging, and the effect exerted by a particular antioxidant bound to it, it is possible to recommend specific food intake or resistance to it to improve the condition or slow down the process.
Language	English
Publishing date	2023-03-27
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2704216-9
ISSN	2076-3921
ISSN	2076-3921
DOI	10.3390/antiox12040815
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating

Radomirovic, Mirjana / Minic, Simeon / Stanic-Vucinic, Dragana / Nikolic, Milan / Van Haute, Sam / Rajkovic, Andreja / Cirkovic Velickovic, Tanja

Food hydrocolloids. 2022 Feb., v. 123

2022

Abstract: β-lactoglobulin (BLG) is a major whey protein with numerous techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), a bioactive pigment of Arthrospira platensis with health-promoting effects, covalently binds to BLG at ... ...

Abstract	β-lactoglobulin (BLG) is a major whey protein with numerous techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), a bioactive pigment of Arthrospira platensis with health-promoting effects, covalently binds to BLG at physiological pH. This study investigated the effects of this covalent modification on BLG functional properties. The BLG–PCB adduct possesses enhanced antioxidant properties, and bound PCB protects BLG against free radical-induced oxidation. Despite the similar thermal stabilities of BLG and BLG–PCB, BLG–PCB is less susceptible to covalent and noncovalent aggregation under moderate heat treatment (63 °C, 30 min). Blocked thiol group and reduced hydrophobicity due to hindering of hydrophobic residues by bound PCB, as well as the heat-induced transition of β-sheet to α-helix, contributed to the low susceptibility of BLG–PCB to aggregation. BLG–PCB has a higher resistance to pepsin and pancreatin digestion than BLG and unaltered IgE-binding properties. The improved functional properties of BLG–PCB make it a useful ingredient in the food industry.
Keywords	Arthrospira platensis ; antioxidants ; chemical bonding ; digestion ; food industry ; health promotion ; heat treatment ; hydrocolloids ; hydrophobicity ; ingredients ; oxidation ; pH ; pancreatin ; pepsin ; thiols ; whey protein
Language	English
Dates of publication	2022-02
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	742742-6
ISSN	1873-7137 ; 0268-005X
ISSN (online)	1873-7137
ISSN	0268-005X
DOI	10.1016/j.foodhyd.2021.107169
Database	NAL-Catalogue (AGRICOLA)

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Bonn / Germany

Z 4414: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article: Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation

Gligorijević, Nikola / Radomirović, Mirjana / Rajković, Andreja / Nedić, Olgica / Ćirković Veličković, Tanja

Foods. 2020 June 12, v. 9, no. 6

2020

Abstract: The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, as it was later discovered that the presence of antioxidants, including ...

Abstract	The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.
Keywords	antioxidant activity ; antioxidants ; bioavailability ; blood coagulation ; coagulation ; environment ; fibrinogen ; fluorescence emission spectroscopy ; food additives ; incidence ; melting point ; oxidation ; polyphenols ; protective effect ; red wines ; resveratrol ; saturated fats ; solubility
Language	English
Dates of publication	2020-0612
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
Note	NAL-light
ZDB-ID	2704223-6
ISSN	2304-8158
ISSN	2304-8158
DOI	10.3390/foods9060780
Database	NAL-Catalogue (AGRICOLA)

Order via subito

Article: Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation.

Gligorijević, Nikola / Radomirović, Mirjana / Rajković, Andreja / Nedić, Olgica / Ćirković Veličković, Tanja

Foods (Basel, Switzerland)

2020 Volume 9, Issue 6

Abstract	The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.
Language	English
Publishing date	2020-06-12
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2704223-6
ISSN	2304-8158
ISSN	2304-8158
DOI	10.3390/foods9060780
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention.

Gligorijevic, Nikola / Radomirovic, Mirjana / Nedic, Olgica / Stojadinovic, Marija / Khulal, Urmila / Stanic-Vucinic, Dragana / Cirkovic Velickovic, Tanja

International journal of molecular sciences

2021 Volume 22, Issue 22

Abstract: The worldwide outbreak of COVID-19 was caused by a pathogenic virus called Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2). Therapies against SARS-CoV-2 target the virus or human cells or the immune system. However, therapies based on ... ...

Abstract	The worldwide outbreak of COVID-19 was caused by a pathogenic virus called Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2). Therapies against SARS-CoV-2 target the virus or human cells or the immune system. However, therapies based on specific antibodies, such as vaccines and monoclonal antibodies, may become inefficient enough when the virus changes its antigenicity due to mutations. Polyphenols are the major class of bioactive compounds in nature, exerting diverse health effects based on their direct antioxidant activity and their effects in the modulation of intracellular signaling. There are currently numerous clinical trials investigating the effects of polyphenols in prophylaxis and the treatment of COVID-19, from symptomatic, via moderate and severe COVID-19 treatment, to anti-fibrotic treatment in discharged COVID-19 patients. Antiviral activities of polyphenols and their impact on immune system modulation could serve as a solid basis for developing polyphenol-based natural approaches for preventing and treating COVID-19.
MeSH term(s)	Antiviral Agents/chemistry ; Antiviral Agents/metabolism ; Antiviral Agents/therapeutic use ; COVID-19/prevention & control ; COVID-19/virology ; Coronavirus 3C Proteases/antagonists & inhibitors ; Coronavirus 3C Proteases/metabolism ; Coronavirus Papain-Like Proteases/antagonists & inhibitors ; Coronavirus Papain-Like Proteases/metabolism ; Humans ; Plants, Medicinal/chemistry ; Plants, Medicinal/metabolism ; Polyphenols/chemistry ; Polyphenols/metabolism ; Polyphenols/therapeutic use ; SARS-CoV-2/isolation & purification ; SARS-CoV-2/metabolism ; Spike Glycoprotein, Coronavirus/antagonists & inhibitors ; Spike Glycoprotein, Coronavirus/metabolism
Chemical Substances	Antiviral Agents ; Polyphenols ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; 3C-like proteinase, SARS-CoV-2 (EC 3.4.22.-) ; Coronavirus Papain-Like Proteases (EC 3.4.22.2) ; papain-like protease, SARS-CoV-2 (EC 3.4.22.2) ; Coronavirus 3C Proteases (EC 3.4.22.28)
Language	English
Publishing date	2021-11-17
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms222212385
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Role of Resveratrol in Prevention and Control of Cardiovascular Disorders and Cardiovascular Complications Related to COVID-19 Disease: Mode of Action and Approaches Explored to Increase Its Bioavailability.

Gligorijević, Nikola / Stanić-Vučinić, Dragana / Radomirović, Mirjana / Stojadinović, Marija / Khulal, Urmila / Nedić, Olgica / Ćirković Veličković, Tanja

Molecules (Basel, Switzerland)

2021 Volume 26, Issue 10

Abstract: Resveratrol is a phytoalexin produced by many plants as a defense mechanism against stress-inducing conditions. The richest dietary sources of resveratrol are berries and grapes, their juices and wines. Good bioavailability of resveratrol is not ... ...

Abstract	Resveratrol is a phytoalexin produced by many plants as a defense mechanism against stress-inducing conditions. The richest dietary sources of resveratrol are berries and grapes, their juices and wines. Good bioavailability of resveratrol is not reflected in its high biological activity in vivo because of resveratrol isomerization and its poor solubility in aqueous solutions. Proteins, cyclodextrins and nanomaterials have been explored as innovative delivery vehicles for resveratrol to overcome this limitation. Numerous in vitro and in vivo studies demonstrated beneficial effects of resveratrol in cardiovascular diseases (CVD). Main beneficial effects of resveratrol intake are cardioprotective, anti-hypertensive, vasodilatory, anti-diabetic, and improvement of lipid status. As resveratrol can alleviate the numerous factors associated with CVD, it has potential as a functional supplement to reduce COVID-19 illness severity in patients displaying poor prognosis due to cardio-vascular complications. Resveratrol was shown to mitigate the major pathways involved in the pathogenesis of SARS-CoV-2 including regulation of the renin-angiotensin system and expression of angiotensin-converting enzyme 2, stimulation of immune system and downregulation of pro-inflammatory cytokine release. Therefore, several studies already have anticipated potential implementation of resveratrol in COVID-19 treatment. Regular intake of a resveratrol rich diet, or resveratrol-based complementary medicaments, may contribute to a healthier cardio-vascular system, prevention and control of CVD, including COVID-19 disease related complications of CVD.
MeSH term(s)	Biological Availability ; COVID-19/complications ; COVID-19/drug therapy ; COVID-19/metabolism ; Cardiovascular Diseases/drug therapy ; Cardiovascular Diseases/etiology ; Cardiovascular Diseases/metabolism ; Humans ; Resveratrol/pharmacokinetics ; Resveratrol/therapeutic use ; SARS-CoV-2/metabolism
Chemical Substances	Resveratrol (Q369O8926L)
Language	English
Publishing date	2021-05-11
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	1413402-0
ISSN	1420-3049 ; 1431-5165 ; 1420-3049
ISSN (online)	1420-3049
ISSN	1431-5165 ; 1420-3049
DOI	10.3390/molecules26102834
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.MO 81: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Phycocyanobilin-modified beta-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating

Radomirovic, Mirjana / Minic, Simeon / Stanic-Vucinic, Dragana / Nikolic, Milan / Van Haute, Sam / Rajkovic, Andreja / Cirkovic Velickovic, Tanja

Food hydrocolloids

2022 Volume 123, Issue -, Page(s) 107169

Language	English
Document type	Article
ZDB-ID	742742-6
ISSN	0268-005X
Database	Current Contents Nutrition, Environment, Agriculture

In stock of ZB MED Bonn / Germany

Z 4414: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c.

Stanic-Vucinic, Dragana / Nikolic, Stefan / Vlajic, Katarina / Radomirovic, Mirjana / Mihailovic, Jelena / Cirkovic Velickovic, Tanja / Grguric-Sipka, Sanja

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry

2020 Volume 25, Issue 2, Page(s) 253–265

Abstract: The reactions of four cymene-capped ruthenium(II) compounds with pro-apoptotic protein, cytochrome c (Cyt), and anti-proliferative protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV-vis absorption, and CD spectroscopy. The ... ...

Abstract	The reactions of four cymene-capped ruthenium(II) compounds with pro-apoptotic protein, cytochrome c (Cyt), and anti-proliferative protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV-vis absorption, and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species, initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO
MeSH term(s)	Coordination Complexes/chemistry ; Cymenes/chemistry ; Cytochromes c/chemistry ; Molecular Conformation ; Muramidase/chemistry ; Muramidase/metabolism ; Ruthenium/chemistry
Chemical Substances	Coordination Complexes ; Cymenes ; Ruthenium (7UI0TKC3U5) ; Cytochromes c (9007-43-6) ; Muramidase (EC 3.2.1.17)
Language	English
Publishing date	2020-02-04
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1464026-0
ISSN	1432-1327 ; 0949-8257
ISSN (online)	1432-1327
ISSN	0949-8257
DOI	10.1007/s00775-020-01758-3
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

Order via subito

Details ▾
- Full text online
- Order with fees

To top

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

Full text online

More links

Kategorien

Order via subito