2018
DOI: 10.1016/j.msec.2018.07.064
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Formulation, characterization, and in vitro/in vivo studies of capsaicin-loaded albumin nanoparticles

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Cited by 46 publications
(21 citation statements)
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“…The second region (1703–1494 cm −1 ) with a high interaction corresponds to the amide I and amide II bands of BSA with the hydrophobic side chain of the capsaicin (Figure 3b, red rectangle). The FTIR results of BSA-capsaicin nanoparticles are completely different when compared with the more recent report of De Freitas et al [17] on the interpretation of the FTIR analysis about the association of the functional groups of capsaicin and BSA molecules in a different context. This interpretation did not explain the relationship of BSA-capsaicin nanostructuration and simplified the interaction through the hydroxyl groups of capsaicin with the sulfhydryl groups of cysteine of BSA, due to the large quantities of BSA molecules found.…”
Section: Resultscontrasting
confidence: 80%
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“…The second region (1703–1494 cm −1 ) with a high interaction corresponds to the amide I and amide II bands of BSA with the hydrophobic side chain of the capsaicin (Figure 3b, red rectangle). The FTIR results of BSA-capsaicin nanoparticles are completely different when compared with the more recent report of De Freitas et al [17] on the interpretation of the FTIR analysis about the association of the functional groups of capsaicin and BSA molecules in a different context. This interpretation did not explain the relationship of BSA-capsaicin nanostructuration and simplified the interaction through the hydroxyl groups of capsaicin with the sulfhydryl groups of cysteine of BSA, due to the large quantities of BSA molecules found.…”
Section: Resultscontrasting
confidence: 80%
“…A similar effect of the concentration of capsaicin was observed by Sánchez-Segura et al [9]; they found that an increase in the capsaicin concentration affected both the yield of BSA nanoparticles, and the efficiency of the drug entrapped in the nanoparticles due to an increased exposure of the hydrophobic sites in the albumin resulting in a major affinity for hydrophobic drugs. De Freitas et al [17] reported that the rate of ethanol addition (1 mL/min) had a higher impact on EE%; they attributed this effect to the process of drug encapsulation which possibly requires lower rate during the desolvation stage. However, they did not put forth a possible mechanism and the effect of the rate on the formation of nanoparticles from the albumin-capsaicin complex.…”
Section: Resultsmentioning
confidence: 99%
“…The spectrum of pure Capsicum oleoresin showed bands around 3100, 2875, 1750, 1500, 750 cm −1 , thus pointing to the presence of an aromatic ring, polar groups (hydroxyl, amide, and carbonyl groups), and a hydrophobic group ( Freitas et al, 2018 ). Aromatic groups, represented in the 3000–3150 cm −1 spectral region, are the most important bands for this oleoresin.…”
Section: Resultsmentioning
confidence: 99%
“…De Freitas et al . 20 reported that BSA-capsaicin nanoparticles stored at freezing conditions (− 4 °C) showed a lower drug release reaching 7% of capsaicin entrapped, compared to NPs stored at room temperature that reached 31% and NPs stored under refrigeration (4 °C) showed 18% of released capsaicin after 3 months.
Figure 2 Encapsulated capsaicin in nanoparticles as a function of initial concentration.
…”
Section: Resultsmentioning
confidence: 99%
“…It is also noticeable that the surface of the NPs was slightly rougher; a similar effect was observed in BSA-capsaicin nanoparticles reported by De Freitas et al . 20 . It is probable that the dual effect of freeze drying and high capsaicin concentrations produced columnar aggregates with quasi-spherical shape.…”
Section: Resultsmentioning
confidence: 99%