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 and Jan KOMÁREK

Basic information

Original name

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

Authors

CZUBINSKI, Jaroslaw (guarantor), Monika KUBÍČKOVÁ (203 Czech Republic, belonging to the institution), Kamil SZPOTKOWSKI and Jan KOMÁREK (203 Czech Republic, belonging to the institution)

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10700 1.7 Other natural sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 10.700 in 2022

Organization unit

Central European Institute of Technology

DOI

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

UT WoS

001101546700001

Keywords in English

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

Abstract

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.

Links

EF18_046/0015974, research and development project

Name: Modernizace České infrastruktury pro integrativní strukturní biologii

LM2023042, research and development project

Name: Česká infrastruktura pro integrativní strukturní biologii

Investor: Ministry of Education, Youth and Sports of the CR, CIISB - Czech Infrastructure for Integrative Structural Biology

Citovat

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

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