Interaction of detergents with bovine lens α-crystallin: evidence for an oligomeric structure based on amphiphilic interactions

Aerts, Tony; Clauwaert, J.; Haezebrouck, Petra; Peeters, Emma; Dael, H. Van

doi:10.1007/s002490050059

Cited by 16 publications

(11 citation statements)

References 41 publications

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“…At regular time intervals, absorption profiles were recorded at 280 nm, first at 20,000 rpm to sediment possible high molecular mass particles and then at 40,000 rpm to sediment tubulin dimers. All measurements were carried out at 23°C, and the data were processed as described elsewhere (Aerts et al, 1997).…”

Section: Analytical Ultracentrifugationmentioning

confidence: 99%

Correct Diffusion Coefficients of Proteins in Fluorescence Correlation Spectroscopy. Application to Tubulin Oligomers Induced by Mg2+ and Paclitaxel

Krouglova

Vercammen

Engelborghs

2004

Biophysical Journal

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In view of recent warnings for artifacts in fluorescence correlation spectroscopy, the diffusion coefficient of a series of labeled proteins in a wide range of molecular mass (43-670 kD) was determined and shown to be correct with respect to published values and the theory. Fluorescence correlation spectroscopy was then applied to the study of fluorescently labeled tubulin and its oligomerization in vitro induced by Mg2+ ions, paclitaxel, and a fluorescent derivative of paclitaxel (Flutax2). By applying relations derived from the theory of Oosawa, we were able to determine the association constant of the oligomers induced by Mg2+. With Flutax2 our experiments show that at nanomolar concentration, the fluorescent derivative is able to recruit tubulin dimers and to form oligomers of defined size. Flutax2 does not bind to microtubules preformed with paclitaxel, but it becomes preferentially incorporated into microtubules when Flutax2 oligomers are preformed, and microtubule formation is induced by paclitaxel addition. This shows that their incorporation into microtubules is faster than the displacement of the prebound drug. Experiments using fluorescently labeled tubulin and (unlabeled) paclitaxel confirm the induction of tubulin oligomers at limiting paclitaxel concentrations.

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Section: Analytical Ultracentrifugationmentioning

confidence: 99%

Correct Diffusion Coefficients of Proteins in Fluorescence Correlation Spectroscopy. Application to Tubulin Oligomers Induced by Mg2+ and Paclitaxel

Krouglova

Vercammen

Engelborghs

2004

Biophysical Journal

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“…Octyl glucoside has been used to study the structure and dynamics of bacteriorhodopsin (41), mammalian rhodopsin (42), OmpF porin from Escherichia coli (43), and the E. coli outer membrane ferrichrome transporter FhuA (44). Extensive biophysical characterizations have shown that octyl glucoside, even at a concentration well above its critical micellar concentration, does not perturb the quaternary structure of the soluble lens protein ␣-crystallin (45,46). Furthermore, oligomerization studies of subunits B777 (47) and B820 (35) of the light-harvesting complex from Rhodobacter sphearoides have been performed in octyl glucoside micelles.…”

mentioning

confidence: 99%

Ligand Binding Promotes the Entropy-driven Oligomerization of Integrin αIIbβ3

Hantgan¹,

Lyles²,

Mallett³

et al. 2003

Journal of Biological Chemistry

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Integrin ␣ IIb ␤ 3 clusters on the platelet surface after binding adhesive proteins in a process that regulates signal transduction. However, the intermolecular forces driving integrin self-association are poorly understood. This work provides new insights into integrin clustering mechanisms by demonstrating how temperature and ligand binding interact to affect the oligomeric state of ␣ IIb ␤ 3 . The ligand-free receptor, solubilized in thermostable octyl glucoside micelles, exhibited a cooperative transition at ϳ43°C, monitored by changes in intrinsic fluorescence and circular dichroism. Both signals changed in a direction opposite to that for global unfolding, and both were diminished upon binding the fibrinogen ␥-chain ligand-mimetic peptide cHArGD. Free and bound receptors also exhibited differential sensitivity to temperature-enhanced oligomerization, as measured by dynamic light scattering, sedimentation velocity, and sedimentation equilibrium. Van't Hoff analyses of dimerization constants for ␣ IIb ␤ 3 complexed with cHArGD, cRGD, or eptifibatide yielded large, favorable entropy changes partly offset by unfavorable enthalpy changes. Transmission electron microscopy showed that ligand binding and 37°C incubation enhanced assembly of integrin dimers and larger oligomers linked by tail-to-tail contacts. Interpretation of these images was aided by threading models for ␣ IIb ␤ 3 protomers and dimers based on the ectodomain structure of ␣ v ␤ 3 . We propose that entropy-favorable nonpolar interactions drive ligand-induced integrin clustering and outside-in signaling.

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“…It has also been used in the regeneration of bacterio rhodopsin in mixed micelles [96] and reactivation of several enzymes by surfactant after treatment with guanidinium chloride [97]. It has also been reported that some aspects of the micelle model of alpha-crystalline can be related to its chaperone activity [98]. Surfactants may also interact with proteins directly by competing for oil-water or air-water interfaces [99] and binding to them, thereby leading to substantial changes in protein conformation.…”

Section: Nonionic Surfactantsmentioning

confidence: 98%

Surfactant–Amino Acid and Surfactant–Surfactant Interactions in Aqueous Medium: a Review

Malik

2015

Appl Biochem Biotechnol

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An overview of surfactant-amino acid interactions mainly in aqueous medium has been discussed. Main emphasis has been on the solution thermodynamics and solute-solvent interactions. Almost all available data on the topic has been presented in a lucid and simple way. Conventional surfactants have been discussed as amphiphiles forming micelles and amino acids as additives and their effect on the various physicochemical properties of these conventional surfactants. Surfactant-surfactant interactions in aqueous medium, various mixed surfactant models, are also highlighted to assess their interactions in aqueous medium. Finally, their applied part has been taken into consideration to interpret their possible uses.

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Interaction of detergents with bovine lens α-crystallin: evidence for an oligomeric structure based on amphiphilic interactions

Cited by 16 publications

References 41 publications

Correct Diffusion Coefficients of Proteins in Fluorescence Correlation Spectroscopy. Application to Tubulin Oligomers Induced by Mg2+ and Paclitaxel

Correct Diffusion Coefficients of Proteins in Fluorescence Correlation Spectroscopy. Application to Tubulin Oligomers Induced by Mg2+ and Paclitaxel

Ligand Binding Promotes the Entropy-driven Oligomerization of Integrin αIIbβ3

Surfactant–Amino Acid and Surfactant–Surfactant Interactions in Aqueous Medium: a Review

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