Characterization of the selected honeybee products based on omics techniques

2019 ◽  
Vol 88 (2) ◽  
pp. 129-132
Author(s):  
Eliza Matuszewska ◽  
Paweł Dereziński ◽  
Agnieszka Klupczyńska ◽  
Agata Światły-Błaszkiewicz ◽  
Szymon Plewa ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Dietary Supplements ◽  
Royal Jelly ◽  
Biologically Active ◽  
Human Organism ◽  
Pharmacological Properties ◽  
Bioactive Components ◽  
Honeybee Venom ◽  
Harmful Effects

to comprehensively characterize honeybee venom, royal jelly, propolis, and pollen, by applying advanced analytical and bioinformatics methodologies. Honeybee products (HBP) contain many bioactive components with both beneficial and harmful effects on the human organism. Nevertheless, the overall composition of the HBP remains not fully investigated. Thus, this research is focused on complementary proteomic and metabolomic characterization of biologically active compounds derived from HBP, regarding their toxicological and pharmacological properties. The objectives of the study will be achieved by the application of up to date mass spectrometry techniques. Due to increasing interest in using of HBP in medicine, this project will contribute to improving the safety of HBP‑derived dietary supplements and drugs.

scholarly journals Bioactives from Bee Products and Accompanying Extracellular Vesicles as Novel Bioactive Components for Wound Healing

Molecules ◽  
2021 ◽  
Vol 26 (12) ◽  
pp. 3770
Author(s):  
Željka Peršurić ◽  
Sandra Kraljević Pavelić
Keyword(s):  
Mass Spectrometry ◽  
Wound Healing ◽  
Chemical Composition ◽  
Extracellular Vesicles ◽  
Royal Jelly ◽  
Geographical Origin ◽  
Bioactive Components ◽  
Animal Cells ◽  
Health Promoting ◽  
High Diversity

In recent years, interest has surged among researchers to determine compounds from bee products such as honey, royal jelly, propolis and bee pollen, which are beneficial to human health. Mass spectrometry techniques have shown that bee products contain a number of proven health-promoting compounds but also revealed rather high diversity in the chemical composition of bee products depending on several factors, such as for example botanical sources and geographical origin. In the present paper, we present recent scientific advances in the field of major bioactive compounds from bee products and corresponding regenerative properties. We also discuss extracellular vesicles from bee products as a potential novel bioactive nutraceutical component. Extracellular vesicles are cell-derived membranous structures that show promising potential in various therapeutic areas. It has been extensively reported that the use of vesicles, which are naturally formed in plant and animal cells, as delivery agents have many advantages. Whether the use of extracellular vesicles from bee products represents a new solution for wound healing remains still to be elucidated. However, promising results in specific applications of the bee products in wound healing and tissue regenerative properties of extracellular vesicles provide a good rationale to further explore this idea.

Characterization of honeybee venom by MALDI-TOF and nanoESI-QqTOF mass spectrometry

2011 ◽  
Vol 54 (2) ◽  
pp. 273-278 ◽  
Author(s):  
Jan Matysiak ◽  
Christian E.H. Schmelzer ◽  
Reinhard H.H. Neubert ◽  
Zenon J. Kokot
Keyword(s):  
Mass Spectrometry ◽  
Honeybee Venom ◽  
Maldi Tof

Towards the Standard-Module Approach to Disulfide-Linked Polypeptide Nanostructures. I. Methodological Prerequisites and Mass Spectrometric Characterization of the Test Two-Loop Structure

2003 ◽  
Vol 9 (2) ◽  
pp. 139-148 ◽  
Author(s):  
O.A. Mirgorodskaya ◽  
K.F. Haselmann ◽  
F. Kjeldsen ◽  
R.A. Zubarev ◽  
P. Roepstorff
Keyword(s):  
Mass Spectrometry ◽  
Disulfide Bonds ◽  
Bond Cleavage ◽  
Bond Formation ◽  
Peptide Bond ◽  
Biologically Active ◽  
Loop Structure ◽  
Partial Acid Hydrolysis ◽  
Peptide Bond Cleavage

Potentially biologically-active nanostructures can be created from single chains of unmodified peptides by cross-linking different regions of the chain by disulfide bonds and cleaving the chain at specified sites to obtain the final configuration. The availability of techniques for assembly and characterization of such structures was tested on a two-loop structure created from a 21-residue linear peptide. Directed intra-molecular disulfide bond formation was performed by inserting partial sequences favoring intra-molecular S–S bond formation (“loops”) separated by partial sequences disfavoring such a process (“spacers”) into the precursor sequence. Peptide bond cleavage by partial acid hydrolysis at specific sites (GG, NP/DP) inside the loops opened them; the same process in the spacer separated the loops. Synthesis, oxidation and bond cleavage were monitored by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI ToF MS). The hydrolysis fragments of the produced nanostructures were characterized by tandem electrospray ionization Fourier transform mass spectrometry (ESI FT-MS) with collisional and electron capture dissociations. The latter technique was especially useful as it cleaves S–S bonds preferentially. The feasibility of the proposed synthesis approach and the adequacy of the analysis techniques for the test structure were demonstrated.

Characterization of the 12% trichloroacetic acid-insoluble oligopeptides of Parmigiano-Reggiano cheese

1992 ◽  
Vol 59 (3) ◽  
pp. 401-411 ◽  
Author(s):  
Francesco Addeo ◽  
Lina Chianese ◽  
Antonio Salzano ◽  
Raffaele Sacchi ◽  
Ugo Cappuccio ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Molecular Mass ◽  
Trichloroacetic Acid ◽  
Fast Atom Bombardment ◽  
Biologically Active ◽  
Isolation And Identification ◽  
Chemical Methods ◽  
Parmigiano Reggiano

SummaryThe isolation and identification of low molecular mass peptides formed during the ripening of Parmigiano-Reggiano cheese is described. A strategy was used based on the fractionation of nitrogenous material using chemical methods followed by HPLC to isolate peptides and fast atom bombardment-mass spectrometry to identify them. It was found that the majority of cheese oligopeptides arose from the proteolysis of β-casein. Several phosphopeptides and oligopeptides known in vivo to be biologically active have also been identified during the ripening of cheese.

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