2018
DOI: 10.1021/acs.jpcb.8b00338
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Probing the Gelatin–Alkylammonium Salt Mixed Assemblies through Surface Tensiometry and Fluorimetry

Abstract: The interactions, nature of the organization, and physicochemical properties of alkyltrimethylammonium bromide (C TAB, n = 12, 14, and 16)-gelatin mixed assemblies were investigated by UV-visible spectrometry, surface tensiometry, and fluorimetry techniques. The synergistic interaction between the surfactant and gelatin was established from the decrease in critical micellar concentration (cmc) and the increase in molecular parking area of surfactants with an increase in percentage of gelatin from 0 to 0.4%; fo… Show more

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Cited by 22 publications
(17 citation statements)
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“…As seen in Figure 1, in the case of the neat gelatin solution, there was an intense and sharp peak at about 300 nm, corresponding to peptide bonds in the gelatin. [ 45, 46 ] In the case of Ag‐G20, that peak shifted to around 330 nm. Ag‐G20 also exhibited a wider peak centered at about 405 nm, indicating formation of the Ag NPs in the solution.…”
Section: Resultsmentioning
confidence: 99%
“…As seen in Figure 1, in the case of the neat gelatin solution, there was an intense and sharp peak at about 300 nm, corresponding to peptide bonds in the gelatin. [ 45, 46 ] In the case of Ag‐G20, that peak shifted to around 330 nm. Ag‐G20 also exhibited a wider peak centered at about 405 nm, indicating formation of the Ag NPs in the solution.…”
Section: Resultsmentioning
confidence: 99%
“…On the other hand, the protein can assume charged or neutral character depending on the pH of its immediate environment and its isoelectric point. For most of the proteins, the isoelectric point lies within 4.8–5.0 [39, 40]. To ascertain the solubilisation site and nature of orientation of the protein present in MDF within an RM, the point of zero charge (PZC) and natural pH of MDF in water were determined (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…This leads to the separation of RMP from the other biomolecules in MDF. Within the water pool, RMP arranges itself to get minimal free‐energy constraints [39, 40, 43]. Consequently, the driving forces for the solubilisation of RMP within the water pool are: (i) the electrostatic attraction between the hydrophilic surfactant (headgroups) of AOT and charged regions of the protein; and (ii) the hydrophobic interactions among the nonpolar segments of the protein.…”
Section: Resultsmentioning
confidence: 99%
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“…Absorption maximum of alginate in water is at ~210 nm 74. Gelatin has two absorption maxima, one corresponds to the presence of peptide bond and side chains of the aromatic groups (π → π* transition) at 220 nm, and the other corresponds to the aromatic side chains (n → π* transition) at 280 nm 75. The absorption maximum of (unmodified) silk fibroin polymer is at 280 nm 76.…”
mentioning
confidence: 99%