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Interaction of γ-conglutin from Lupinus albus with model phospholipid membranes: Investigations on structure, thermal stability and oligomerization status.
- Source :
-
BBA - Proteins & Proteomics . Dec2018, Vol. 1866 Issue 12, p1242-1248. 7p. - Publication Year :
- 2018
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Abstract
- Abstract Interaction with model phospholipid membranes of lupin seed γ-conglutin, a glycaemia-lowering protein from Lupinus albus seeds, has been studied by means of Fourier-Transform infrared spectroscopy at p2H 7.0 and at p2H 4.5. The protein maintains the same secondary structure both at p2H 7.0 and at p2H 4.5, but at p2H 7.0 a higher 1H/2H exchange was observed, indicating a greater solvent accessibility. The difference in T m and T D1/2 of the protein at the abovementioned p2H's has been calculated around 20 °C. Infrared measurements have been then performed in the presence of DMPG and DOPA at p2H 4.5. DMPG showed a little destabilizing effect while DOPA exerted a great stabilizing effect, increasing the T m of γ-conglutin at p2H 4.5 of more than 20 °C. Since γ-conglutin at p2H 4.5 is in the monomeric form, the interaction with DOPA likely promotes the oligomerization even at p2H 4.5. Interaction between DMPG or DOPA and γ-conglutin has been confirmed by turbidity experiments with DMPC:DMPG or DOPC:DOPA SUVs. Turbidity data also showed high-affinity binding of γ-conglutin to anionic SUVs made up with DOPA. The molecular features outlined in this study are relevant to address the applicative exploitation and to delineate a deeper comprehension of the natural functional role of γ-conglutin. Highlights • γ-conglutin when orally administered in humans and animals significantly decrease glycaemia. • Structure, thermal stability, interaction and oligomerization status with SUVs has been studied by spectroscopic method. • DOPA exerts a great stabilizing effect on thermal stability, probably by promoting oligomerization. • High-affinity binding of γ-conglutin to anionic SUVs with DOPA has been observed. • Stabilizing and protective effects of SUVs may be useful carriers for nutraceutical applications of γ-conglutin. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 15709639
- Volume :
- 1866
- Issue :
- 12
- Database :
- Academic Search Index
- Journal :
- BBA - Proteins & Proteomics
- Publication Type :
- Academic Journal
- Accession number :
- 132549407
- Full Text :
- https://doi.org/10.1016/j.bbapap.2018.10.005