Binding interactions of cationic gemini surfactants with gold nanoparticles-conjugated bovine serum albumin: A FRET/NSET, spectroscopic, and docking study

Halder, Sayantan; Aggrawal, Rishika; Jana, Srabanti; Saha, Sarani

doi:10.1016/j.jphotobiol.2021.112351

Cited by 19 publications

(47 citation statements)

References 108 publications

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“…Refolding of the unfolded conjugated AuNPs-BSA has been carried out at a concentration of 0.2 mM each of gemini surfactant, 12-4-12,2Br − and 12-8-12,2Br − based on our previous reports. 13 Fig. S1 † shows the binding isotherm to display binding between the conjugated AuNPs-BSA and gemini surfactants based on changes in fluorescence intensity and α-helix% with an increase in surfactant concentration.…”

Section: Resultsmentioning

confidence: 99%

“…Zetasizer Nano-ZS 90 from Malvern Instruments Ltd was used for DLS measurements. 13 The Milli-Q water was first filtered with 0.22 μm pore size filter paper (Millipore) and that was used to prepare the buffer solution. This buffer solution filtered with the same filter paper was then used to prepare BSA, gemini surfactant and SDS solutions.…”

Section: Methodsmentioning

confidence: 99%

“…The sample preparation for FT-IR measurements, its parameters and instrumental details have been reported earlier. 13 Each measurement was recorded three times and the corresponding standard deviations obtained are given in the relevant figures and tables accordingly. The temperature was kept fixed at 298.15 ± 1 K for all measurements.…”

Section: Methodsmentioning

confidence: 99%

“…Earlier, the unfolding of the conjugated AuNPs-BSA has been carried out by these two cationic gemini surfactants and demonstrated by the FRET/NSET method. 13 After the consolidation of the gemini surfactant-BSA binding isotherm, the refolding study of unfolded bioconjugated protein using SDS through the formation of catanion/mixed assemblies with gemini surfactant has been performed by the FRET and NSET methods. On interacting with cationic gemini surfactant molecules, SDS molecules form catanion due to the oppositely charged headgroups.…”

Section: Introductionmentioning

confidence: 99%

“…It is well established in our previous report that the protein's helicity is majorly retained even after bioconjugation in its native as well as unfolded states. 13 The ionic surfactants have a strong affinity to bind to the proteins stepwise. Thus, a detailed picture of the protein–surfactant interactions is presented here.…”

Section: Introductionmentioning

confidence: 99%

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Refolding of denatured gold nanoparticles-conjugated bovine serum albumin through formation of catanions between gemini surfactant and sodium dodecyl sulphate

et al. 2022

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Refolding of denatured gold nanoparticles-conjugated bovine serum albumin through formation of catanions between gemini surfactant and sodium dodecyl sulphate

et al. 2022

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N‐lauroylglutamates with two and four carboxylate head groups: Their interactions with bovine serum albumin

Singh,

Gupta,

Neelakshi

et al. 2024

J Surfact & Detergents

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N‐lauroyl derivatives of amino acids have widely been reported as environmentally benign surfactants. Although N‐lauroyl‐l‐glutamate is reported in the literature, the effect of the two carboxylate groups in it has not been specifically addressed. In this study, we report the interactions of bovine serum albumin (BSA) with N‐lauroylglutamate (S1) and an N‐lauroyl derivative of a tripeptide of glutamic acid (S2), respectively. The surfactant S1 has two and S2 has four carboxylic acid groups making them different from other N‐lauroyl amino acids, which have just one carboxylic acid group. The aim of this study is to understand the role of the number of carboxylate groups present in these amino acid‐based anionic surfactants while interacting with biomolecules such as BSA. The critical micelle concentration (CMC) of the surfactants were measured both in the presence and absence of BSA using fluorescence spectroscopy. The fluorescence of BSA was quenched on addition of the surfactants. The mechanisms of fluorescence quenching were established by studying the fluorescence at three different temperatures. CD studies were performed to calculate the temperature at which BSA unfolds completely in the presence and absence of the surfactants. Conformational changes in the secondary structure of BSA were also observed on the addition of S1 and S2. The results of these studies are compared with those previously reported for the interactions between BSA and N‐lauroylglycinate. We find that S1 has a lower CMC than S2 and lauroylglycinate. The surfactant S1 stabilized the secondary structure of BSA better at higher temperatures.

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Nanozymes as Catalytic Marvels for Biomedical and Environmental Concerns: A Chemical Engineering Approach

BS,

Babu

et al. 2023

J Clust Sci

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Binding interactions of cationic gemini surfactants with gold nanoparticles-conjugated bovine serum albumin: A FRET/NSET, spectroscopic, and docking study

Cited by 19 publications

References 108 publications

Refolding of denatured gold nanoparticles-conjugated bovine serum albumin through formation of catanions between gemini surfactant and sodium dodecyl sulphate

Refolding of denatured gold nanoparticles-conjugated bovine serum albumin through formation of catanions between gemini surfactant and sodium dodecyl sulphate

N‐lauroylglutamates with two and four carboxylate head groups: Their interactions with bovine serum albumin

Nanozymes as Catalytic Marvels for Biomedical and Environmental Concerns: A Chemical Engineering Approach

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