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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F24%3A00135416" target="_blank" >RIV/00216224:14740/24:00135416 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/pii/S0268005X23009323?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0268005X23009323?via%3Dihub</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.foodhyd.2023.109386" target="_blank" >10.1016/j.foodhyd.2023.109386</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10400 - Chemical sciences

Projekt

<a href="/cs/project/EF18_046%2F0015974" target="_blank" >EF18_046/0015974: Modernizace České infrastruktury pro integrativní strukturní biologii</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2024

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Food Hydrocolloids

ISSN

0268-005X

e-ISSN

1873-7137

Svazek periodika

147

Číslo periodika v rámci svazku

A

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

1-12

Kód UT WoS článku

001101546700001

EID výsledku v databázi Scopus

2-s2.0-85173823528