Effective Critical Micellar Concentration of a Zwitterionic Detergent: A Fluorimetric Study on n-Dodecyl Phosphocholine

Palladino, Pasquale; Rossi, Filomena; Ragone, Raffaele

doi:10.1007/s10895-009-0537-0

Cited by 37 publications

(37 citation statements)

References 38 publications

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“…S1). Therefore, our simulation data support the existence of detergent-mediated protein aggregation in the presence of salt, although we note that chloride ions (used in these simulations) differ from phosphate ions (used by Hwang et al (Hwang et al, 2002) for NMR), and salt concentrations up to 7 M affect the critical micelle concentration of DPC (Palladino et al, 2010).…”

Section: Aggregated Statessupporting

confidence: 69%

Detergent-mediated protein aggregation

Neale

Ghanei

Holyoake

et al. 2013

Chemistry and Physics of Lipids

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Because detergents are commonly used to solvate membrane proteins for structural evaluation, much attention has been devoted to assessing the conformational bias imparted by detergent micelles in comparison to the native environment of the lipid bilayer. Here, we conduct six 500-ns simulations of a system with >600,000 atoms to investigate the spontaneous self assembly of dodecylphosphocholine detergent around multiple molecules of the integral membrane protein PagP. This detergent formed equatorial micelles in which acyl chains surround the protein's hydrophobic belt, confirming existing models of the detergent solvation of membrane proteins. In addition, unexpectedly, the extracellular and periplasmic apical surfaces of PagP interacted with the headgroups of detergents in other micelles 85 and 60% of the time, respectively, forming complexes that were stable for hundreds of nanoseconds. In some cases, an apical surface of one molecule of PagP interacted with an equatorial micelle surrounding another molecule of PagP. In other cases, the apical surfaces of two molecules of PagP simultaneously bound a neat detergent micelle. In these ways, detergents mediated the non-specific aggregation of folded PagP. These simulation results are consistent with dynamic light scattering experiments, which show that, at detergent concentrations ≥600 mM, PagP induces the formation of large scattering species that are likely to contain many copies of the PagP protein. Together, these simulation and experimental results point to a potentially generic mechanism of detergent-mediated protein aggregation.

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Section: Aggregated Statessupporting

confidence: 69%

Detergent-mediated protein aggregation

Neale

Ghanei

Holyoake

et al. 2013

Chemistry and Physics of Lipids

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“…Titration with DPC Suggests Surface Interactions-Addition of aliquots from a concentrated solution of DPC into a 1 mM 15 N CHR peptide at pH 7.6 was carried out by making sure that the first addition yielded a concentration of DPC (14 mM) in the sample that is well above the critical micelle concentration (1.1 mM) of DPC in pure water (29,30). Measurement of the critical micelle concentration of DPC using 31 P NMR showed that the chemical shift of the headgroup phosphorous reached the value associated with a micellar environment at 3-4 mM (30).…”

Section: Resultsmentioning

confidence: 99%

Interactions between the Conserved Hydrophobic Region of the Prion Protein and Dodecylphosphocholine Micelles

Sauvé

Buijs

Gingras

et al. 2012

Journal of Biological Chemistry

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The three-dimensional structure of PrP110 -136, a peptide encompassing the conserved hydrophobic region of the human prion protein, has been determined at high resolution in dodecylphosphocholine micelles by NMR. The results support the conclusion that the Ctm PrP, a transmembrane form of the prion protein, adopts a different conformation than the reported structures of the normal prion protein determined in solution. Paramagnetic relaxation enhancement studies with gadolinium-diethylenetriaminepentaacetic acid indicated that the conserved hydrophobic region peptide is not inserted symmetrically in the micelle, thus suggesting the presence of a guanidium-phosphate ion pair involving the side chain of the terminal arginine and the detergent headgroup. Titration of dodecylphosphocholine into a solution of PrP110 -136 revealed the presence of a surface-bound species. In addition, paramagnetic probes located the surface-bound peptide somewhere below the micelle-water interface when using the inserted helix as a positional reference. This localization of the unknown population would allow a similar ion pair interaction.

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“…In the case of zwitterionic DPC, this effect is less pronounced because of the overall neutral charge of the surfactant. Therefore, it is proposed that the drop in the cmc of DPC might be due to salting out and the implication of phosphocholine headgroups in organization of the surrounding water molecules [42]. It is worth noting that for the 9:1 DPC/SDS system, the change in cmc observed upon transfer from the unbuffered to buffered solution is negligible (taking into account cmc1 in PBS).…”

Section: Mixed Micelles In Unbuffered Solutionmentioning

confidence: 99%

Thermodynamics, size, and dynamics of zwitterionic dodecylphosphocholine and anionic sodium dodecyl sulfate mixed micelles

Sikorska

Wyrzykowski

Szutkowski

et al. 2015

J Therm Anal Calorim

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The thermodynamic properties of micellization for dodecylphosphocholine (DPC), sodium dodecyl sulfate (SDS), and their mixtures were studied using isothermal titration calorimetry. NMR relaxation measurements were used to explore molecular mobility of the DPC-containing micelles, whereas the diffusion measurements were taken to determine the micelle size. The DPC/SDS mixed systems reveal a tendency to form two kinds of micelles in buffered solution at lower temperatures. An increase in temperature as well as the transfer of the DPC/SDS mixed micelles from buffered to unbuffered solution results in only a single-step micellization process. The average size of the DPC-containing micelles is only slightly dependent on the SDS fraction. Examination of the data of spin-spin relaxation (T 2 ) shows that methylene protons on the polar headgroup of DPC and methylene protons (H1) on the hydrocarbon chain in the micellar systems studied reveal a heterogeneous dynamic behavior reflected in a twocomponent T 2 relaxation in the whole temperature range. The latter is the main constituent of the rigid interfacial layer core protecting the penetration of water into the hydrophobic interior.

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Effective Critical Micellar Concentration of a Zwitterionic Detergent: A Fluorimetric Study on n-Dodecyl Phosphocholine

Cited by 37 publications

References 38 publications

Detergent-mediated protein aggregation

Detergent-mediated protein aggregation

Interactions between the Conserved Hydrophobic Region of the Prion Protein and Dodecylphosphocholine Micelles

Thermodynamics, size, and dynamics of zwitterionic dodecylphosphocholine and anionic sodium dodecyl sulfate mixed micelles

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