The effect of protein stability on protein–monoglyceride interactions

Boots, J.W.P.; Chupin, Vladimir; Killian, J. Antoinette; Demel, R.A.; Kruijff, Ben de

doi:10.1016/s0009-3084(02)00049-x

Cited by 5 publications

(1 citation statement)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…They exhibit sharp X-ray diffraction patterns and optical birefringence. [6][7][8][9][10][11][12][13][14][15] At higher temperatures, the coagels turn into either micellar solutions or gel phases, depending on the length of the hydrophobic chain of the surfactant. 16 The coagel-tomicelle and coagel-to-gel transitions of these ASCn/water systems have been studied by scanning differential calorimetry (DSC).…”

Section: Introductionmentioning

confidence: 99%

Water of hydration in coagels

Ambrosi

Nostro

Fratoni

et al. 2004

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

Vitamin C-based alkanoyl-6-O-ascorbic acid esters, ASCn, are a class of surfactants, interesting both on account of their phase behaviour, and of the properties of the supramolecular assemblies they form. When dispersed in water at room, or lower, temperatures above ca. 5% w/w concentration, they form coagels. At higher temperatures, the microstructure changes to micellar solutions for surfactants of low hydrocarbon chain length n. The longer chained systems form gel phases. The transition enthalpy change is dominated by rearrangements in hydrophobic chain packing. On the other hand the Krafft point seems instead to be dictated mainly by interactions between the polar headgroups and the solvent. The coagel phase is usually thought of as formed of surfactant lamellae separated by thin interlayers of strongly bound, essentially '' frozen '', water molecules. In this work, DSC measurements were performed to explore the interactions between water and the surfactant molecules. Two kinds of water were detected: interlayer hydration water and bulk water. The number of hydration water molecules per polar headgroup was inferred from the experimental results. Further insights into the coagel structure were gained from X-ray diffraction and optical microscopy. The effects of glycerin (GLY), propylene glycol (PG), and poly(ethylene glycol) (PEG), as co-solvents were investigated by conductivity and DSC experiments. Glycerin seems to stabilize the coagel, probably through the formation of hydrogen bonds that compete for the polar headgroups with the strongly bound water molecules. By contrast, PG and PEG decrease the compactness of the lamellar structure. This is most likely because these compounds can penetrate into the lipid portion of the lamellae, and reduce the hydrophobic interactions that hold the compact assemblies together.

show abstract

Section: Introductionmentioning

confidence: 99%

Water of hydration in coagels

Ambrosi

Nostro

Fratoni

et al. 2004

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

show abstract

Comparative analysis of the electrostatics of the binding of cationic proteins to vesicles: Asymmetric location of anionic phospholipids

Torrens

Castellano

2009

Analytica Chimica Acta

View full text Add to dashboard Cite

Streptomyces chromofuscus phospholipase D interaction with lipidic activators at the air–water interface

Kirat

Chauvet

Roux

et al. 2004

Biochimica et Biophysica Acta (BBA) - Biomembranes

View full text Add to dashboard Cite

The phospholipase D from Streptomyces chromofuscus (PLDSc) is a soluble enzyme that interacts with membranes to catalyse phosphatidylcholine (PC) transformation. In this work, we focused on the interaction between PLDSc and two lipid activators: a neutral lipid, diacylglycerol (DAG), and an anionic one, phosphatidic acid (PA). DAG is a naturally occurring alcohol, so it is a potent nucleophile for the transphosphatidylation reaction catalysed by PLD. Concerning PA, it is a widely described activator of PLDSc-catalysed hydrolysis of PC. The monolayer technique allowed us to define PLDSc interaction with DAG and PA. In the case of DAG, the results suggest an insertion of PLDSc within the acyl chains of the lipid with an exclusion pressure of approximately 45 mN/m. PLDSc-DAG interaction seemed to occur preferentially with the lipid in the liquid-expanded (LE) phase. PLDSc interaction with PA was found to be more effective at high surface pressures. The overall results obtained with PA show a preferential interaction of the protein with condensed PA domains. No exclusion pressure could be found for PLDSc-PA interaction indicating only superficial interaction with the polar head of this lipid. Brewster angle microscopy (BAM) images were acquired in order to confirm these results and to visualise the patterns induced by PLDSc adsorption.

show abstract

The effect of protein stability on protein–monoglyceride interactions

Cited by 5 publications

References 14 publications

Water of hydration in coagels

Water of hydration in coagels

Comparative analysis of the electrostatics of the binding of cationic proteins to vesicles: Asymmetric location of anionic phospholipids

Streptomyces chromofuscus phospholipase D interaction with lipidic activators at the air–water interface

Contact Info

Product

Resources

About