2009
DOI: 10.1016/j.jpba.2008.11.035
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Study of curcumin and genistein interactions with human serum albumin

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Cited by 199 publications
(83 citation statements)
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“…These results were in agreement with Zhongfa et al who reported that PEG400 was capable of solubilizing curcumin to a higher extent (Zhongfa et al, 2012). W.W. Quitschke (2012) explained the solubilization power of PEG by its amphiphilic properties confirming Mandeville et al (2009) andSun et al (2008) observations that curcumin requires hydrophobic and hydrophilic moieties balance, in addition they described the solubility behavior of curcumin as amphipathic.…”
Section: Solubility Studysupporting
confidence: 91%
“…These results were in agreement with Zhongfa et al who reported that PEG400 was capable of solubilizing curcumin to a higher extent (Zhongfa et al, 2012). W.W. Quitschke (2012) explained the solubilization power of PEG by its amphiphilic properties confirming Mandeville et al (2009) andSun et al (2008) observations that curcumin requires hydrophobic and hydrophilic moieties balance, in addition they described the solubility behavior of curcumin as amphipathic.…”
Section: Solubility Studysupporting
confidence: 91%
“…This wide structural variation, including their substituents, has given to polyphenols their different levels of anti-AGEs and anti-diabetic activities demonstrated in vivo and in vitro studies (Xie et al, 2013;Klein et al, 2011b). While the original paradigm indicated the antiglycative effect of polyphenols was due to their free radical scavenging potential, new evidence of scavenging-independent protection has emerged (Vlassopoulos et al, 2013;Sadowska-Bartosz et al, 2014;Mandeville et al, 2009). …”
Section: Introductionmentioning
confidence: 99%
“…Human serum albumin (HSA) with high affinity binding sites is a major transporter for delivering several endogenous compounds and drugs in vivo. Structural analysis showed that genistein binds to HSA via polypeptide polar groups (Mandeville et al, 2009). Binding of genistein to albumins is reversible, rapid and the concentration of unbound isoflavone is in an equilibrium state.…”
Section: Binding Of Genistein To Different Proteinsmentioning
confidence: 99%