A new method for quantitative determination of renalase based on mass spectrometric determination of a proteotypic peptide labelled with stable isotopes

Kopylov, Arthur T.; Fedchenko, V. I.; Buneeva, O. A.; Pyatakova, N. V.; Zgoda, Victor G.; Медведев, А. Е.

doi:10.1002/rcm.8167

Cited by 7 publications

(2 citation statements)

References 21 publications

(61 reference statements)

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“…LC–MS/MS and HPLC were utilized to quality and quantify connexin43 mimetic peptide, exhibiting therapeutic effects in managing inflammatory eye conditions and spinal cord injury (Bisht et al., 2017). Additional quantification approaches involve the use of radioisotopes (Forrer et al., 2007), stable isotopes (Kopylov et al., 2018), fluorescent, and chemiluminescence reagents (Rezgui et al., 2016). Meanwhile, enzymes can quantify peptides by biological chemical analysis of their catalytic activities (Aydin, 2015).…”

Section: Extraction Purification and Analysis Methods Of Fbpsmentioning

confidence: 99%

Recent progress of food‐derived bioactive peptides: Extraction, purification, function, and encapsulation

Jiang,

Sun,

Chandrapala

et al. 2024

Food Frontiers

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Functional peptides constitute a class of small molecular peptide chains with specific functions in biology and are typically composed of various amino acids. The chemical‐synthesis methods for preparation of functional peptides can bring high toxicity to the human body. Therefore, there is a growing need to explore alternative, safter sources to obtain bioactive peptides. Food‐derived bioactive peptides (FBPs) stand out as an ideal substitution offering safety and accessibility that can be used in health products and pharmaceuticals to elicit their effects. Presently, the extraction, purification, functional properties, and bioavailability of FBPs have been poorly summarized. This review aims to address this gap by summarizing key aspects of FBPs, covering their source, methods of preparation, extraction, isolation, purification, and identification. Additionally, the review explores the functional characteristics and mechanism underlying FBPs. Emphasis is placed on strategies to enhance the stability and bioaccessibility of FBPs, crucial for their successful application in the food and medical industries. Existing research findings suggest that adopting appropriate methods can extract FBPs with high yield and purity. FBPs exhibit both in vitro and in vivo biological activities regulating relevant pathways, showcasing their potential in the medical field. In the quest for improved stability, the application of nanomaterials emerges as a promising strategy. These advancements collectively hint at a bright future for FBPs in both food and medical matrices. As the field progresses, further exploration and refinement of extraction techniques, functional properties, and bioavailability will contribute to unlocking the full potential of FBPs in various applications.

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Section: Extraction Purification and Analysis Methods Of Fbpsmentioning

confidence: 99%

Recent progress of food‐derived bioactive peptides: Extraction, purification, function, and encapsulation

Jiang,

Sun,

Chandrapala

et al. 2024

Food Frontiers

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“…Затем кодирующую последовательность химерного гена RNLS человека без N-концевого пептида, не содержащую в гене стоп кодон, вставляли по сайтам рестрикции BamHI/ XhoI в вектор pET-28a (+) которым трансформировали клетки E. coli Rosetta (DE3 [20], также подтвердил присутствие химерного белка в трансфицированных клетках (и его отсутствие в контрольных, нетрансфицированных клетках).…”

Section: результаты и обсуждениеunclassified

Construction of a chimeric human gene encoding renalase with a modified N-terminus

Fedchenko

Kaloshin

Kozlova

et al. 2020

BMCRM

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Renalase (RNLS) is a recently discovered protein that plays different roles inside and outside cells. Extracellular RNLS exhibits protective effects on the cell, acting on its receptor proteins, while intracellular RNLS acts as FAD-dependent oxidoreductase (EC 1.6.3.5). The ratio of the intracellular and extracellular forms of this protein, as well as the mechanisms and factors responsible for its transport from the cell, remain unknown. One of the approaches to studying these issues can be the creation of chimeric forms of this protein with modified fragments of its amino acid sequences. This work describes a method for constructing a chimeric human RNLS gene encoding RNLS without its N-terminal peptid

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Is renalase ready to become a biomarker of ischemia?

Медведев

Kopylov

Fedchenko

et al. 2020

International Journal of Cardiology

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A new method for quantitative determination of renalase based on mass spectrometric determination of a proteotypic peptide labelled with stable isotopes

Cited by 7 publications

References 21 publications

Recent progress of food‐derived bioactive peptides: Extraction, purification, function, and encapsulation

Recent progress of food‐derived bioactive peptides: Extraction, purification, function, and encapsulation

Construction of a chimeric human gene encoding renalase with a modified N-terminus

Is renalase ready to become a biomarker of ischemia?

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