pH-Dependent oligomerisation of γ-conglutin: A key element to
understand its molecular mechanism of action

J 2024

pH-Dependent oligomerisation of γ-conglutin: A key element to understand its molecular mechanism of action

CZUBINSKI, Jaroslaw, Monika KUBÍČKOVÁ, Kamil SZPOTKOWSKI a Jan KOMÁREK

Základní údaje

Originální název

pH-Dependent oligomerisation of γ-conglutin: A key element to understand its molecular mechanism of action

Autoři

CZUBINSKI, Jaroslaw (garant), Monika KUBÍČKOVÁ (203 Česká republika, domácí), Kamil SZPOTKOWSKI a Jan KOMÁREK (203 Česká republika, domácí)

Vydání

Food Hydrocolloids, Oxford, Elsevier Science, 2024, 0268-005X

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10700 1.7 Other natural sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 10.700 v roce 2022

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1016/j.foodhyd.2023.109386

UT WoS

001101546700001

Klíčová slova anglicky

gamma-Conglutin; Lupin seed; Oligomerisation; Protein structure; Protein size and molecular weight; Nutraceutical protein

Štítky

CF BIC, CF CRYO, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 16. 7. 2024 20:39, Mgr. Eva Dubská

Anotace

V originále

Despite extensive research carried out on lupin seed gamma-conglutin neither its mechanism of action as a hypoglycaemic nutraceutical compound nor its physiological role for the plant has been unveil. This article revealed a pH-dependent reversible association/dissociation equilibrium involving monomer, dimer and hexamer of Lupinus angustifolius gamma-conglutin. The interaction between different oligomeric forms of this protein is reversible, and spectroscopic studies showed that the intact structure of gamma-conglutin was preserved under the tested environmental conditions tested (pH 4.5-7.5). The obtained results prove that the hexameric form was preferred under basic conditions and was stabilised by a number of bonds formed upon association of individual protomers. The simultaneous occurrence of several oligomeric forms at a given pH value was shown, and their share was strongly driven by protein concentration. The main changes in oligomerisation of gamma-conglutin take place in a pH range of 4.5-6.0, correlating with the pKa(R) values of the amino acid residues of His (6.0), Glu (4.1), and Asp (3.9). Moreover, a structural model of the protein in hexamer assembly was obtained based on small-angle X-ray scattering (SAXS) and negative staining cryo-electron microscopy (cryo-EM) analyses. The presented study provides essential knowledge about the colloidal dynamics and stability of gamma-conglutin in solution, improving our understanding of fundamental environmental factors that could affect the health-promoting activity of this lupin seed protein.

Návaznosti

EF18_046/0015974, projekt VaV

Název: Modernizace České infrastruktury pro integrativní strukturní biologii

LM2023042, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CIISB - Česká infrastruktura pro integrativní strukturní biologii

Citovat

CZUBINSKI, Jaroslaw, Monika KUBÍČKOVÁ, Kamil SZPOTKOWSKI a Jan KOMÁREK. pH-Dependent oligomerisation of γ-conglutin: A key element to understand its molecular mechanism of action. Food Hydrocolloids. Oxford: Elsevier Science, 2024, roč. 147, A, s. 1-12. ISSN 0268-005X. Dostupné z: https://dx.doi.org/10.1016/j.foodhyd.2023.109386.

@article{2367497,
   author = {Czubinski, Jaroslaw and Kubíčková, Monika and Szpotkowski, Kamil and Komárek, Jan},
   article_location = {Oxford},
   article_number = {A},
   doi = {http://dx.doi.org/10.1016/j.foodhyd.2023.109386},
   keywords = {gamma-Conglutin; Lupin seed; Oligomerisation; Protein structure; Protein size and molecular weight; Nutraceutical protein},
   language = {eng},
   issn = {0268-005X},
   journal = {Food Hydrocolloids},
   title = {pH-Dependent oligomerisation of γ-conglutin: A key element to understand its molecular mechanism of action},
   url = {https://www.sciencedirect.com/science/article/pii/S0268005X23009323?via%3Dihub},
   volume = {147},
   year = {2024}
}

TY  - JOUR
ID  - 2367497
AU  - Czubinski, Jaroslaw - Kubíčková, Monika - Szpotkowski, Kamil - Komárek, Jan
PY  - 2024
TI  - pH-Dependent oligomerisation of γ-conglutin: A key element to understand its molecular mechanism of action
JF  - Food Hydrocolloids
VL  - 147
IS  - A
SP  - 1-12
EP  - 1-12
PB  - Elsevier Science
SN  - 0268005X
KW  - gamma-Conglutin
KW  - Lupin seed
KW  - Oligomerisation
KW  - Protein structure
KW  - Protein size and molecular weight
KW  - Nutraceutical protein
UR  - https://www.sciencedirect.com/science/article/pii/S0268005X23009323?via%3Dihub
N2  - Despite extensive research carried out on lupin seed gamma-conglutin neither its mechanism of action as a hypoglycaemic nutraceutical compound nor its physiological role for the plant has been unveil. This article revealed a pH-dependent reversible association/dissociation equilibrium involving monomer, dimer and hexamer of Lupinus angustifolius gamma-conglutin. The interaction between different oligomeric forms of this protein is reversible, and spectroscopic studies showed that the intact structure of gamma-conglutin was preserved under the tested environmental conditions tested (pH 4.5-7.5). The obtained results prove that the hexameric form was preferred under basic conditions and was stabilised by a number of bonds formed upon association of individual protomers. The simultaneous occurrence of several oligomeric forms at a given pH value was shown, and their share was strongly driven by protein concentration. The main changes in oligomerisation of gamma-conglutin take place in a pH range of 4.5-6.0, correlating with the pKa(R) values of the amino acid residues of His (6.0), Glu (4.1), and Asp (3.9). Moreover, a structural model of the protein in hexamer assembly was obtained based on small-angle X-ray scattering (SAXS) and negative staining cryo-electron microscopy (cryo-EM) analyses. The presented study provides essential knowledge about the colloidal dynamics and stability of gamma-conglutin in solution, improving our understanding of fundamental environmental factors that could affect the health-promoting activity of this lupin seed protein.
ER  -

CZUBINSKI, Jaroslaw, Monika KUBÍČKOVÁ, Kamil SZPOTKOWSKI a Jan KOMÁREK. pH-Dependent oligomerisation of γ-conglutin: A key element to understand its molecular mechanism of action. \textit{Food Hydrocolloids}. Oxford: Elsevier Science, 2024, roč.~147, A, s.~1-12. ISSN~0268-005X. Dostupné z: https://dx.doi.org/10.1016/j.foodhyd.2023.109386.

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