Gold nanoparticles (AuNPs) are considered useful vehicles for medical therapy and diagnosis. Despite the progress made in this field, there is need to find direct, reliable, and versatile synthetic procedures for their preparation as well as new multifunctional coating agents. In this sense, we have explored the use of imidazolium amphiphiles to prepare new AuNPs designed for anion recognition and transport. Thus, in this work we describe (a) the synthesis, by a phase transfer method, of new gold nanoparticles using gemini-type surfactants as ligands based on imidazolium salts, those ligands acting as transfer agents into organic media and also as nanoparticle stabilizers, (b) the examination of their stability in solution, (c) the chemical and physical characterization of the nanoparticles, using a variety of techniques, including UV-visible spectroscopy (UV-vis), transmission electron microscopy (TEM), and X-ray photoelectron spectroscopy (XPS), (d) toxicity data concerning both the imidazolium ligands and the imidazolium coated nanoparticles, (e) the assessment of their molecular recognition ability toward molecules of biological interest, such as anions and carboxylate containing model drugs, such as ibuprofen, (f) the study of their toxicity and those of their coating ligands, as well as their ability for cell internalization, and (g) the study of their ability for delivering anionic pharmaceuticals. The structurally governed triple role of those new gemini-type surfactants is responsible for the preparation, remarkable stability, and delivery properties of these functional AuNPs.
The
globular protein γB-crystallin exhibits a
complex phase behavior, where liquid–liquid phase separation
characterized by a critical volume fraction ϕc =
0.154 and a critical temperature Tc =
291.8 K coexists with dynamical arrest on all length scales at volume
fractions around ϕ ≈ 0.3–0.35, and an arrest line
that extends well into the unstable region below the spinodal. However,
although the static properties such as the osmotic compressibility
and the static correlation length are in quantitative agreement with
predictions for binary liquid mixtures, this is not the case for the
dynamics of concentration fluctuations described by the dynamic structure
factor S(q,t).
Using a combination of dynamic light scattering and neutron spin echo
measurements, we demonstrate that the competition between critical
slowing down and dynamical arrest results in a much more complex wave
vector dependence of S(q,t) than previously anticipated.
Investigating proteins with techniques such as NMR or neutron scattering frequently requires the partial or complete substitution of D2O for H2O as a solvent, often tacitly assuming that such a solvent substitution does not significantly alter the properties of the protein. Here, we report a systematic investigation of the solvent isotope effect on the phase diagram of the lens protein γB-crystallin in aqueous solution as a model system exhibiting liquid-liquid phase separation. We demonstrate that the observed strong variation of the critical temperature Tc can be described by the extended law of corresponding states for all H2O/D2O ratios, where scaling of the temperature by Tc or the reduced second virial coefficient accurately reproduces the binodal, spinodal, and osmotic compressibility. These findings highlight the impact of H2O/D2O substitution on γB-crystallin properties and warrant further investigations into the universality of this phenomenon and its underlying mechanisms.
Although small round gold nanoparticles (Au NPs) possess only a small degree of shape anisotropy, they support localized surface plasmon resonances and exhibit intrinsic optical anisotropy. These inherent features promote depolarized light scattering, whose temporal fluctuations carry information about rotational Brownian dynamics, and thus can be used to describe the size distribution of round Au NPs. We demonstrate that this allows for a much more accurate determination of particle size and polydispersity through depolarized dynamic light scattering when compared to standard particle sizing with light scattering.
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