| 1. |
- Bayati, Solmaz, et al.
(author)
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Complexes of PEO-PPO-PEO triblock copolymer P123 and bile salt sodium glycodeoxycholate in aqueous solution : A small angle X-ray and neutron scattering investigation
- 2016
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In: Colloids and Surfaces A: Physicochemical and Engineering Aspects. - : Elsevier BV. - 0927-7757. ; 504, s. 426-436
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Journal article (peer-reviewed)abstract
- Small angle X-ray (SAXS) and neutron scattering techniques were combined to study mixed complexes formed between micelles of the nonionic amphiphilic PEO-PPO-PEO copolymer (P123) and the anionic bile salt (NaGDC) in aqueous solution. The purpose was to investigate the structural parameters of the charged complexes, such as size and internal structure, as well as their interparticle interactions in aqueous solution. The overall aim of this work was to gain understanding of how thermoresponsive PEO-PPO-PEO block copolymers interact with bile salts in order to make predictions as to whether they can be put forward as a new class of bile salt sequestrants in the treatment of bile-salt related diseases. The system was investigated at a constant P123 concentration of 1.74 mM and bile salt concentrations were varied up to a molar ratio [Formula presented] (MR) = 5.7. It was found that the NaGDC molecules preferentially associated to the PEO corona of the P123 micelle and due to their amphiphilic nature, close to the core/corona interface. Because of this association the micelles became charged causing their reciprocal interparticle repulsions in solution to increase. In parallel, the association caused a decrease in the core radius accompanied by dehydration, which in turn led to a decrease in total radius of the “P123 micelle-NaGDC” complexes. To elucidate the effect of the interactions on their diffusive motion, an interaction model based on a spherical particle with a hard-core interaction shell was employed using the fitted SAXS data. At higher molar ratios, the interparticle interaction was increasingly screened because of nonadsorbed bile salt in the surrounding solution. Meanwhile, a further decrease in total radial size of the P123 micelle-NaGDC complexes occurred due to a decrease in the aggregation number of P123 as the bile salt finally disintegrated the complexes. However, the micelles were found to be more stable and less prone to disintegration in D2O. This investigation demonstrated the importance of using small angle scattering techniques for studying intermolecular interactions in order to gain understanding of how natural surfactants influence the aggregation behavior of amphiphilic polymers.
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| 2. |
- Bayati, Solmaz, et al.
(author)
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Effects of Bile Salt Sodium Glycodeoxycholate on the Self-Assembly of PEO-PPO-PEO Triblock Copolymer P123 in Aqueous Solution.
- 2015
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In: Langmuir. - : American Chemical Society (ACS). - 0743-7463 .- 1520-5827. ; 31:50, s. 13519-13527
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Journal article (peer-reviewed)abstract
- A comprehensive experimental study on the interaction between the PEO-PPO-PEO block copolymer P123 (EO20PO68EO20) and the anionic bile salt sodium glycodeoxycholate (NaGDC) in water has been performed. The work was aimed at investigating the suitability of using P123 as bile salt sequestrant beside the fundamental aspects of PEO-PPO-PEO block copolymer-bile salt interactions. Various experimental techniques including dynamic and static light scattering, small-angle X-ray scattering, and differential scanning calorimetry (DSC) were employed in combination with electrophoretic mobility measurements. The system was investigated at a constant P123 concentration of 1.74 mM and with varying bile salt concentrations up to approximately 250 mM NaGDC (or a molar ratio nNaGDC/nP123 = 144). In the mixed P123-NaGDC solutions, the endothermic process related to the self-assembly of P123 was observed to gradually decrease in enthalpy and shift to higher temperatures upon progressive addition of NaGDC. To explain this effect, the formation of NaGDC micelles carrying partly dehydrated P123 unimers was proposed and translated into a stoichiometric model, which was able to fit the experimental DSC data. In the mixtures at low molar ratios, NaGDC monomers associated with the P123 micelle forming a charged "P123 micelle-NaGDC" complex with a dehydrated PPO core. These complexes disintegrated upon increasing NaGDC concentration to form small "NaGDC-P123" complexes visualized as bile salt micelles including one or a few P123 copolymer chains.
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| 3. |
- BAYATI, SOLMAZ, et al.
(author)
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Mixed micelles of oppositely charged poly(N-isopropylacrylamide) diblock copolymers
- 2017
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In: Journal of Polymer Science, Part B: Polymer Physics. - : Wiley. - 0887-6266. ; 55:19, s. 1457-1470
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Journal article (peer-reviewed)abstract
- Mixed micelle formation between two oppositely charged diblock copolymers that have a common thermosensitive nonionic block of poly(N-isopropylacrylamide) (PNIPAAM) has been studied. The block copolymer mixed solutions were investigated under equimolar charge conditions as a function of both temperature and total polymer concentrations by turbidimetry, differential scanning calorimetry, two-dimensional proton nuclear magnetic nuclear Overhauser effect spectroscopy (2D 1H NMR NOESY), dynamic light scattering, and small angle X-ray scattering measurements. Well-defined and electroneutral cylindrical micelles were formed with a radius and a length of about 3 nm and 35 nm, respectively. In the micelles, the charged blocks built up a core, which was surrounded by a corona of PNIPAAM chains. The 2D 1H NMR NOESY experiments showed that a minor block mixing occurred between the core blocks and the PNIPAAM blocks. By approaching the lower critical solution temperature of PNIPAAM, the PNIPAAM chains collapsed, which induced aggregation of the micelles.
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| 4. |
- Cautela, Jacopo, et al.
(author)
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C-12 vs C-3 substituted bile salts : An example of the effects of substituent position and orientation on the self-assembly of steroid surfactant isomers
- 2020
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In: Colloids and Surfaces B: Biointerfaces. - : Elsevier BV. - 0927-7765. ; 185
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Journal article (peer-reviewed)abstract
- Biomolecule derivatives are transversally used in nanotechnology. Deciphering their aggregation behavior is a crucial issue for the rational design of functional materials. To this end, it is necessary to build libraries of selectively functionalized analogues and infer general rules. In this work we enrich the highly applicative oriented collection of steroid derivatives, by reporting a rare example of C-12 selectively modified bile salt. While nature often exploits such position to encode functions, it is unusual and not trivial to prepare similar analogues in the laboratory. The introduction of a tert-butyl phenyl residue at C-12 provided a molecule with a self-assembly that remarkably switched from rigid pole-like structures to twisted ribbons at a biologically relevant critical temperature (∼25 °C). The system was characterized by microscopy and spectroscopy techniques and compared with the C-3 functionalized analogue. The twisted ribbons generate samples with a gel texture and a viscoelastic response. The parallel analysis of the two systems suggested that the observed thermoresponsive self-assemblies occur at similar critical temperatures and are probably dictated by the nature of the substituent, but involve aggregates with different structures depending on position and orientation of the substituent. This study highlights the self-assembly properties of two appealing thermoresponsive systems. Moreover, it adds fundamental insights hereto missing in the investigations of the relation between self-assembly and structure of synthetic steroids, which are valuable for the rational design of steroidal amphiphiles.
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| 5. |
- Cautela, Jacopo, et al.
(author)
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Supracolloidal Atomium
- 2020
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In: ACS Nano. - : American Chemical Society (ACS). - 1936-086X .- 1936-0851. ; 14:11, s. 15748-15756
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Journal article (peer-reviewed)abstract
- Nature suggests that complex materials result from a hierarchical organization of matter at different length scales. At the nano- and micrometer scale, macromolecules and supramolecular aggregates spontaneously assemble into supracolloidal structures whose complexity is given by the coexistence of various colloidal entities and the specific interactions between them. Here, we demonstrate how such control can be implemented by engineering specially customized bile salt derivative-based supramolecular tubules that exhibit a highly specific interaction with polymeric microgel spheres at their extremities thanks to their scroll-like structure. This design allows for hierarchical supracolloidal self-assembly of microgels and supramolecular scrolls into a regular framework of “nodes” and “linkers”. The supramolecular assembly into scrolls can be triggered by pH and temperature, thereby providing the whole supracolloidal system with interesting stimuli-responsive properties. A colloidal smart assembly is embodied with features of center-linker frameworks as those found in molecular metal–organic frameworks and in structures engineered at human scale, masterfully represented by the Atomium in Bruxelles.
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| 6. |
- Del Giudice, Alessandra, et al.
(author)
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Self-Assembly of Model Amphiphilic Peptides in Nonaqueous Solvents : Changing the Driving Force for Aggregation Does Not Change the Fibril Structure
- 2020
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In: Langmuir. - : American Chemical Society (ACS). - 0743-7463 .- 1520-5827. ; 36:29, s. 8451-8460
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Journal article (peer-reviewed)abstract
- Within the homologous series of amphiphilic peptides AnK, both A8K and A10K self-assemble in water to form twisted ribbon fibrils with lengths around 100 nm. The structure of the fibrils can be described in terms of twisted β-sheets extending in the direction of the fibrils, laminated to give a constant cross section of 4 nm by 8 nm. The finite width of the twisted ribbons can be reasonably explained within a simple thermodynamic model, considering a free energy penalty for the stretching of hydrogen bonds along the twisted β-sheets and an interfacial free energy gain for the lamination of the hydrophobic β-sheets. In this study, we characterize the self-assembly behavior of these peptides in nonaqueous solutions as a route to probe the role of hydrophobic interaction in fibril stabilization. Both peptides, in methanol and N,N-dimethylformamide, were found to form fibrillar aggregates with the same β-sheet structure as in water but with slightly smaller cross-sectional sizes. However, the gel-like texture, the slow relaxation in dynamic light scattering experiments, and a correlation peak in the small-angle X-ray scattering pattern highlighted enhanced interfibril interactions in the nonaqueous solvents in the same concentration range. This could be ascribed to a higher effective volume of the aggregates because of enhanced fibril growth and length, as suggested by light scattering and cryogenic transmission electron microscopy analyses. These effects can be discussed considering how the solvent properties affect the different energetic contributions (hydrophobic, electrostatic, and hydrogen bonding) to fibril formation. In the analyzed case, the decreased hydrogen bonding propensity of the nonaqueous solvents makes the hydrogen bond formation along the fibril a key driving force for peptide assembly, whereas it represents a nonrelevant contribution in water.
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| 7. |
- Del Giudice, Alessandra, et al.
(author)
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Structural response of human serum albumin to oxidation : Biological buffer to local formation of hypochlorite
- 2016
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In: Journal of Physical Chemistry B. - : American Chemical Society (ACS). - 1520-6106 .- 1520-5207. ; 120:40, s. 12261-12271
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Journal article (peer-reviewed)abstract
- The most abundant plasma protein, human serum albumin (HSA), plays a key part in the body's antioxidant defense against reactive species. This study was aimed at correlating oxidant-induced chemical and structural effects on HSA. Despite the chemical modification induced by the oxidant hypochlorite, the native shape is preserved up to oxidant/HSA molar ratio <80, above which a structural transition occurs in the critical range 80-120. This conformational variation involves the drifting of one of the end-domains from the rest of the protein and corresponds to the loss of one-third of the α-helix and a net increase of the protein negative charge. The transition is highly reproducible suggesting that it represents a well-defined structural response typical of this multidomain protein. The ability to tolerate high levels of chemical modification in a folded or only partially unfolded state, as well as the stability to aggregation, provides albumin with optimal features as a biological buffer for the local formation of oxidants. (Graph Presented).
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| 8. |
- Del Giudice, Alessandra, et al.
(author)
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The effect of fatty acid binding in the acid isomerizations of albumin investigated with a continuous acidification method
- 2018
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In: Colloids and Surfaces B: Biointerfaces. - : Elsevier BV. - 0927-7765. ; 168, s. 109-116
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Journal article (peer-reviewed)abstract
- The protein Human Serum Albumin (HSA) is known to undergo conformational transitions towards partially unfolded forms triggered by acidification below pH 4.5. The extent of Fatty Acids (FA) binding has been thought to have an impact on the conformational equilibrium between the native and acid forms and to be a possible explanation for the observation of more than one band in early electrophoretic migration experiments at pH 4. We compared the acid-induced unfolding processes of commercial FA-free HSA, commercial “fatted” HSA and FA-HSA complexes, prepared at FA:HSA molar ratios between 1 and 6 by simple mixing and equilibration. We used a method for continuous acidification based on the hydrolysis of glucono-δ-lactone from pH 7 to pH 2.5, and followed the average protein changes by the blue shift of the intrinsic fluorescence emission and by performing a small angle X-ray scattering analysis on selected samples. The method also allowed for continuous monitoring of the increase of turbidity and laser light scattering of the protein samples related to the release of the insoluble ligands with acidification. Our results showed that the presence of FA interacting with albumin, an aspect often neglected in biophysical studies, affects the conformational response of the protein to acidification, and slightly shifts the loss of the native shape from pH 4.2 to pH 3.6. This effect increased with the FA:HSA molar ratio so that with three molar equivalents a saturation was reached, in agreement with the number of high-affinity binding sites reported for the FA. These findings confirm that a non-uniform level of ligand binding in an albumin sample can be an explanation for the early-observed conformational heterogeneity at pH 4.
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| 9. |
- Del Giudice, Alessandra, et al.
(author)
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Time-Dependent pH Scanning of the Acid-Induced Unfolding of Human Serum Albumin Reveals Stabilization of the Native Form by Palmitic Acid Binding
- 2017
-
In: Journal of Physical Chemistry B. - : American Chemical Society (ACS). - 1520-6106 .- 1520-5207. ; 121:17, s. 4388-4399
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Journal article (peer-reviewed)abstract
- The most abundant plasma protein, human serum albumin (HSA), is known to undergo several conformational transitions in an acidic environment. To avoid buffer effects and correlate global and local structural changes, we developed a continuous acidification method and simultaneously monitored the protein changes by both small-angle scattering (SAXS) and fluorescence. The progressive acidification, based on the hydrolysis of glucono-δ-lactone from pH 7 to pH 2.5, highlighted a multistep unfolding involving the putative F form (pH 4) and an extended and flexible conformation (pH < 3.5). The scattering profile of the F form was extracted by component analysis and further 3D modeled. The effect of acid unfolding at this intermediate stage was assigned to the rearrangement of the three albumin domains drifting apart toward a more elongated conformation, with a partial unfolding of one of the outer domains. To test the stabilizing effect of fatty acids, here palmitic acid, we compared the acid unfolding process of albumin with and without ligand. We found that when binding the ligand, the native conformation was favored up to lower pH values. Our approach solved the problem of realizing a continuous, homogeneous, and tunable acidification with simultaneous characterization applicable to study processes triggered by a pH decrease.
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| 10. |
- di Gregorio, Maria Chiara, et al.
(author)
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pH Sensitive Tubules of a Bile Acid Derivative: a Tubule Opening by Release of Wall Leaves
- 2013
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In: Physical Chemistry Chemical Physics. - 1463-9084. ; 15:20, s. 7560-7566
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Journal article (peer-reviewed)abstract
- Tubules formed by self-assembly of organic molecules have a vast potential in nanotechnology applications and the introduction of sensitivity to stimuli into self-assembly tubules represents a particularly attractive feature. Here we report on the preparation and characterization of a molecule obtained by chemical modification of a natural bile acid, a biological surfactant, that self-assembles in pH sensitive tubules in aqueous solutions. The tubules, that are rigid, single-walled and with a diameter of 60 nm, form at pH 8-9 and open up when the pH is increased. The transition is reversible, it occurs in the pH range of 9-10 with an opening mechanism that is remarkably different from those so far proposed in the literature. It involves a release of wall layers similar to leaves, and is determined by a drastic pH-triggered change in the molecular arrangement, which in turn induces a radical modification of the wall curvature. The description of the morphological transformation is performed by means of cryogenic transmission electron microscopy and represent, to our knowledge, the first detailed visualization of pH stimulated tubule opening. UV and circular dichroism spectroscopies are used to investigate the evolution at the molecular level.
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