Self-assembled micellar clusters based on Triton-X-family surfactants for enhanced solubilization, encapsulation, proteins permeability control, and anticancer drug delivery
“…The General Procedure of the Triton-X based MCs formation procedures is described in [1] and is based on the works [2] , [3] , [4] , [5] , [6] , [7] .…”
Section: Experimental Design Materials and Methodsmentioning
The data presented here refer to a research article entitled “Self-Assembled Micellar Clusters Based on Triton-X-family Surfactants for Enhanced Solubilization, Encapsulation, Proteins Permeability Control, and Anticancer Drug Delivery” Solomonov et al., 2019. The present article provides the General Procedure for clusterization of Triton-X-based micelles and the effect of (i) metal ion, surfactant, and chelator concentration on the developed clusters formation, (ii) surfactant-chelator relation change, (iii) metal ion-micelles concertation ratio variation, (iv) metal ion replacement, (v) solvent replacement, (vi) kinetics of clusters formation, (vii) hydrophobic fluorescent dye (Coumarin 6) solubilization in aqueous MCs media, (viii) novel anticancer peptidyl drug synthesis and characterization and (ix) the viability of HeLa cells with and without the presence of drug-free Triton-X-based family MCs. These data provide additional insights useful for understanding all aspects of the micellar clusters formation, optimization, and control.
“…The General Procedure of the Triton-X based MCs formation procedures is described in [1] and is based on the works [2] , [3] , [4] , [5] , [6] , [7] .…”
Section: Experimental Design Materials and Methodsmentioning
The data presented here refer to a research article entitled “Self-Assembled Micellar Clusters Based on Triton-X-family Surfactants for Enhanced Solubilization, Encapsulation, Proteins Permeability Control, and Anticancer Drug Delivery” Solomonov et al., 2019. The present article provides the General Procedure for clusterization of Triton-X-based micelles and the effect of (i) metal ion, surfactant, and chelator concentration on the developed clusters formation, (ii) surfactant-chelator relation change, (iii) metal ion-micelles concertation ratio variation, (iv) metal ion replacement, (v) solvent replacement, (vi) kinetics of clusters formation, (vii) hydrophobic fluorescent dye (Coumarin 6) solubilization in aqueous MCs media, (viii) novel anticancer peptidyl drug synthesis and characterization and (ix) the viability of HeLa cells with and without the presence of drug-free Triton-X-based family MCs. These data provide additional insights useful for understanding all aspects of the micellar clusters formation, optimization, and control.
“…The effects of composition of surfactant on stability of metal complex species of L-methionine are presented in Figure 1 are in good agreement with this concept. Effect of co-solvent interactions in molecular levels can be investigated by this study [ 53 , 54 , 55 , 56 ]. Figure 1 Change in stability of Metal-Met complexes in TX 100-water system: (a) Co II , (b) Ni II , and (c) Cu II …”
The present work aims to evaluate the binding capacities of binary complexes of L-Methionine with transition metal ions Co
II
, Ni
II
and Cu
II
in Triton X 100-water mixtures, a non-ionic micellar media of different compositions (0.0–2.5% (v/v)), investigated under the experimental conditions of 0.16 mol/dm
3
ionic strength using NaNO
3
at a temperature of 303.0 ± 0.1 K Potentiometrically. The potentiometric data was assessed by Irving-Rossotti pH metric technique with the least-squares method of MINIQUAD75, a computer program. The selectivity of the best fit model obtained by continuous exhaustive chemical modelling studies and the accuracy of the results is assessed based on statistical parameters. MLH, ML and ML
2
are the identified species for the three M(Co
II
, Ni
II
and Cu
II
) - Met systems. The shift in the equilibrium of binary metal-methionine complexes with variation in composition (0.0–2.5%) of the solvent can be explained by electrostatic together with non-electrostatic forces contributed by the interaction of solute with solvent.
“…[84] The same group reported dual specific recognition with biotinÀ avidin and hemoproteinÀ heme, which have been used to design nanowires of apomyoglobin, hemoprotein, and streptavidin with alternating alignment ( Figure 4B). [85] Based on interactions with small host-guest molecules, such as cucurbit [8]urils (CB 8 ), [86] Liu et al have obtained a functional highly stable protein nanowire with potential antioxidant properties.…”
Section: D-materials: Protein Strings Rings and Fibrilsmentioning
confidence: 99%
“…[78] The negatively charged cages can encapsulate RNA or superparamagnetic iron oxide nanoparticles, and the superlattices are formed through tunable electrostatic interactions with positively charged gold nanoparticles. Gold nanoparticles (AuNPs) and viruses form an AB (8) fcc (face -central cubic) crystal structure that is not isostructural with any known atomic or molecular crystal structure and it has previously been observed only with large colloidal polymer particles. AuNPs and empty or nanoparticle-loaded ferritin cages form an interpenetrating simple cubic AB structure (isostructural to CsCl).…”
Section: D-materials: Cages Polyhedrons and Capsidsmentioning
confidence: 99%
“…[4][5][6] The formed structures could be easily used as building blocks for designing biomaterials with diverse functionalities. [7,8] Self-assembly has been widely used in chemistry, biology, and materials science as a "bottom-up" approach for developing highly ordered structures at the nanoto micrometer scale with controllable levels of complexity. [4,9] In particular, the self-assembly of peptides and proteins has always been the focus of intensive research, [10][11][12][13][14] especially in developing bio- [15] and composite [16] materials.…”
Supramolecular self‐assembled structures, based on protein−protein interactions, have garnered widespread interest as prospective functional bionanomaterials. Possessing unique properties, proteins have been widely investigated in the last years, due to their capability to form a diversity of natural and artificially designed zero‐, one‐, two‐ and three‐dimensional assemblies. These structures laid the basis for bionanomaterials design, including films, foams, gels, and others, with widespread applications in electronics, biomedicine, and environmental sciences. In this context, the present review is devoted to revealing the diversity of protein assemblies and related bionanomaterials. Special interest is paid to recent advances and new trends in functional amyloids and fibrillar silk‐based self‐assembling architectures, as well as their current and potential applications. We emphasize the protein nanostructures’ diversity for the future design of functional protein‐based materials.
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