THE INTERACTIONS MELAFEN AND IHFANs WITH ANIMAL’S SOLUBLE PROTEIN

O M Alekseeva; Yu A Kim; G E Zaikov

UDC

577.1.04; 577.15.03

THE INTERACTIONS MELAFEN AND IHFANS WITH ANIMAL’S SOLUBLE PROTEIN THE INTERACTIONS MELAFEN AND IHFANs WITH ANIMAL’S SOLUBLE PROTEIN

АА Аа

Published in Herald of Technological University · Pages 164–169 · Rubric: BIOHIMIYa, BIOTEHNOLOGIYa I EKOLOGIYa

Received: 20.04.2023 Accepted: 01.08.2025 Published: 01.08.2025 Language of publication: ENG

Authors

O M Alekseeva

Yu A Kim

G E Zaikov

O M Alekseeva

Emanuel Institute of Biochemical Physics, Russian Academy of Sciences

Yu A Kim

Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino

G E Zaikov

KNRTU

ABSTRACT

The main goal of this work was the investigation of the action of two types of biological active substances to the soluble proteins that enriched the animal’s blood serum. The first task was the test of the influence of plant growth regulator, applied in agriculture, - Melafen (melamine salt of bis (oximethyl) phosphinic acid), to the structural properties of soluble protein - bovine serum albumin (BSA). Melafen was used as the aqua solutions in the wide region of concentration (10 -21 - 10 -3 M). The Melafen interactions with BSA were tested by the spectral methods: BSA absorptions and intrinsic fluorescence of BSA tryptophane residues. We did not reveal any noticeable structural changes of the BSA molecules under the concentrations of Melafen that used at crop production. Melafen has not any destruction’s influences to the soluble proteins structure under the concentrations that activate the plant growth (10-18 - 10 -10 M). The second task was the investigation of the influence of hybrid antioxidants IHFANs that was expected to use as neuroprotector, to the BSA structure properties. IHFANs were used as the aqua-ethanol suspensions in the wide region of concentration (10-21 - 10 -3 M). IHFANs protect from the destruction of BSA molecule, when the ultra low and low concentrations (10-18 - 10 -10 M), by absorbing its alkyl tails at albumin surface. But the “loosening” of molecule BSA structure occurred, when the large concentrations (10-5 - 10 -3 M) of Melafen were presented at medium for intrinsic BSA fluorescence registration. But IHFANs, when the large concentrations (10-5 - 10 -3 M), not only decreased the intrinsic BSA fluorescence, but IHFANs shifted the fluorescence maximum to more short-wavelength. This indicates the initiation of more polar state of environment for BSA tryptophane residues.

KEYWORDS

Melafen, hybrid antioxidant, bovine serum albumin, fluorescence, Мелафен, гибридные антиоксиданты, бычий сывороточный альбумин, флуоресценция

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Alekseeva O. M., Kim Y. A., Zaikov G. E. THE INTERACTIONS MELAFEN AND IHFANs WITH ANIMAL’S SOLUBLE PROTEIN // Herald of Technological University. 2025. no. 7. pp. 164-169. (Date of access 07.09.2026).

MLA

O M Alekseeva, Kim Y. A., Zaikov G. E.. "THE INTERACTIONS MELAFEN AND IHFANs WITH ANIMAL’S SOLUBLE PROTEIN." Herald of Technological University 17.7 (2025): 164-169.

APA

Alekseeva O. M., Kim Y. A., Zaikov G. E. (2025). THE INTERACTIONS MELAFEN AND IHFANs WITH ANIMAL’S SOLUBLE PROTEIN. Herald of Technological University, 17(7), 164-169.

Chicago

O M Alekseeva, Kim Y. A., Zaikov G. E.. "THE INTERACTIONS MELAFEN AND IHFANs WITH ANIMAL’S SOLUBLE PROTEIN." Herald of Technological University 17, no. 7 (2025): 164-169.

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{{cite journal | author = Alekseeva O. M., Kim Y. A., Zaikov G. E. | title = THE INTERACTIONS MELAFEN AND IHFANs WITH ANIMAL’S SOLUBLE PROTEIN | journal = Herald of Technological University | year = 2025 | volume = 17 | issue = 7 | pages = 164-169 }}

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THE INTERACTIONS MELAFEN AND IHFANS WITH ANIMAL’S SOLUBLE PROTEIN THE INTERACTIONS MELAFEN AND IHFANs WITH ANIMAL’S SOLUBLE PROTEIN

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