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Is Gum Arabic a Good Emulsifier Due to CH...? Interactions? How Urea Effectively Destabilizes the Hydrophobic CH...? Interactions in the Proteins of Gum Arabic than Amides and GuHCl?

ABSTRACT: The photophysical studies of gum arabic (GA) in the presence of urea, 1,3-dimethylurea (DMU), tetramethylurea (TMU), guanidine hydrochloride (GuHCl), formamide (FA), acetamide (AA), and dimethyl formamide (DMF) were carried out by monitoring the emission, three-dimensional emission contour, and time-correlated fluorescence lifetime techniques. On addition of only 1 × 10-3 M urea, 75.0% of the fluorescence of GA is quenched, while the same occurs in GuHCl at 3.0 M. FA quenched 50% of the fluorescence of GA at 5.0 M. However, DMU, TMU, AA, and DMF resulted in a fluorescence enhancement. The unusual fluorescence trends reveal the existence of CH...? interactions in the proteins of GA. The experimental results and the structural aspects of proteins in GA led us to propose that the aggregation of polyproline helices in GA, through several CH...? interactions, would have a major role to play in the emulsification mechanism of GA.

SUBMITTER: Sethuraman S

PROVIDER: S-EPMC6787882 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

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Is Gum Arabic a Good Emulsifier Due to CH...π Interactions? How Urea Effectively Destabilizes the Hydrophobic CH...π Interactions in the Proteins of Gum Arabic than Amides and GuHCl?

Sethuraman Sowmiya S Rajendran Kumaran K

ACS omega 20190925 15

The photophysical studies of gum arabic (GA) in the presence of urea, 1,3-dimethylurea (DMU), tetramethylurea (TMU), guanidine hydrochloride (GuHCl), formamide (FA), acetamide (AA), and dimethyl formamide (DMF) were carried out by monitoring the emission, three-dimensional emission contour, and time-correlated fluorescence lifetime techniques. On addition of only 1 × 10<sup>-3</sup> M urea, 75.0% of the fluorescence of GA is quenched, while the same occurs in GuHCl at 3.0 M. FA quenched 50% of t ...[more]

PMID: 31616820

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Project description:Despite extensive research efforts focusing on tackling membrane biofouling, one of the biggest problems associated with membrane technology, there has been little headway in this area. This study presents novel polyethersulfone (PES) membranes synthesized via a phase inversion method at incremental loadings of functionalized oxidized multiwalled carbon nanotubes (OMWCNT) along with 1 wt. % arabic gum (AG). The synthesized OMWCNT were examined using scanning electron microscopy and transmission electron microscopy for morphological changes compared to the commercially obtained carbon nanotubes. Additionally energy-dispersive X-ray spectroscopy was carried out on the raw and OMWCNT materials, indicating an almost 2-fold increase in oxygen content in the latter sample. The cast PES/OMWCNT membranes were extensively characterized, and underwent a series of performance testing using bovine serum albumin solution for fouling tests and model Gram-positive (Bacillus subtilis) and Gram-negative (Escherichia coli) bacterial species for anti-biofouling experiments. Results indicated that the composite PES membranes, which incorporated the OMWCNT and AG, possessed significantly stronger hydrophilicity and negative surface charge as evidenced by water contact angle and zeta potential data, respectively, when compared to plain PES membranes. Furthermore atomic force microscopy analysis showed that the PES/OMWCNT membranes exhibited significantly lower surface roughness values. Together, these membrane surface features were held responsible for the anti-adhesive nature of the hybrid membranes seen during biofouling tests. Importantly, the prepared membranes were able to inhibit bacterial colonization upon incubation with both Gram-positive and Gram-negative bacterial suspensions. The PES/OMWCNT membranes also presented more resilient normalized flux values when compared to neat PES and commercial membrane samples during filtration of both bacterial suspensions and real treated sewage effluents. Taken together, the results of this study allude to OMWCNT and AG as promising additives, for incorporation into polymeric membranes to enhance biofouling resistance.

Project description:Proline residues have unique roles in protein folding, structure, and function. Proline and the aromatic amino acids comprise the encoded cyclic protein residues. Aromatic protein side chains are defined by their negatively charged ? faces, while the faces of the proline ring are partially positively charged. This polarity results from their two-point connection of the side chain to the electron-withdrawing protein backbone, and the lower electronegativity of hydrogen compared to carbon, nitrogen, and oxygen. The hydrogens adjacent to the carbonyl and amide nitrogen, H? and H?, respectively, are the most partially positive. Proline's side chain is also conformationally restricted, allowing for interaction with aromatic residues with minimal entropic or steric penalty. Proline and aromatic residues can interact favorably with each other, due to both the hydrophobic effect and the interaction between the ? aromatic face and the polarized C-H bonds, called a CH/? interaction. Aromatic-proline interactions can occur locally, for example, to stabilize cis-amide bonds, and over larger distances, in the tertiary structures of proteins, and intermolecularly in protein-protein interactions. In peptides and proteins, aromatic-proline sequences more readily adopt cis-prolyl amide bonds, where the aromatic ring interacts with the proline ring in the cis conformation. In aromatic-proline sequences, Trp and Tyr are more likely to induce cis-amide bonds than Phe, suggesting an aromatic electronic effect. This result would be expected for a CH/? interaction, in which a more electron-rich aromatic would have a stronger (more cis-stabilizing) interaction with partial positive charges on prolyl hydrogens. In this Account, we describe our investigations into the nature of local aromatic-proline interactions, using peptide models. We synthesized a series of 26 peptides, TXPN, varying X from electron-rich to electron poor aromatic amino acids, and found that the population of cis-amide bond (Ktrans/cis) is tunable by aromatic electronics. With 4-substituted phenylalanines, we observed a Hammett correlation between aromatic electronics and Ktrans/cis, with cis-trans isomerism electronically controllable by 1.0 kcal/mol. All aromatic residues exhibit a higher cis population than Ala or cyclohexylalanine, with Trp showing the strongest aromatic-proline interaction. In addition, proline stereoelectronic effects can modulate cis-trans isomerism by an additional 1.0 kcal/mol. The aromatic-proline interaction is enthalpic, consistent with its description as a CH/? interaction. Proline-aromatic sequences can also promote cis-prolyl bonds, either through interactions of the aromatic ring with the preceding cis-proline or with the H? prior to cis-proline. Within proline-rich peptides, sequences commonly found in natively disordered proteins, aromatic residues promote multiple cis-amide bonds due to multiple favorable aromatic-proline interactions. Collectively, we found aromatic-proline interactions to be significantly CH/? in nature, tunable by aromatic electronics. We discuss these data in the context of aromatic-proline and aromatic-glycine interactions in local structure, in tertiary structure, in protein-protein interactions, and in protein assemblies.

Dataset Information

Is Gum Arabic a Good Emulsifier Due to CH...? Interactions? How Urea Effectively Destabilizes the Hydrophobic CH...? Interactions in the Proteins of Gum Arabic than Amides and GuHCl?

Publications

Is Gum Arabic a Good Emulsifier Due to CH...π Interactions? How Urea Effectively Destabilizes the Hydrophobic CH...π Interactions in the Proteins of Gum Arabic than Amides and GuHCl?

Similar Datasets

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