2008
DOI: 10.1002/adfm.200800860
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Self‐Assembling Peptide as a Potential Carrier for Hydrophobic Anticancer Drug Ellipticine: Complexation, Release and In Vitro Delivery

Abstract: The self‐assembling peptide EAK16‐II is capable of stabilizing hydrophobic compounds to form microcrystal suspensions in aqueous solution. Here, the ability of this peptide to stabilize the hydrophobic anticancer agent ellipticine is investigated. The formation of peptide‐ellipticine suspensions is monitored with time until equilibrium is reached. The equilibration time is found to be dependent on the peptide concentration. When the peptide concentration is close to its critical aggregation concentration, the … Show more

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Cited by 90 publications
(97 citation statements)
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“…Several hydrophobic anticancer drugs (e.g., paclitaxel, 23 ellipticine, 24,25 curcumin, 26 etc.) have been attempted to be released by (RADA) 4 or other similar ioncomplementary self-assembling peptides (e.g., EAK16-IV, EAK16-II and EFK-II, 24,27−29 MAX8, 30,31 etc.).…”
Section: Introductionmentioning
confidence: 99%
“…Several hydrophobic anticancer drugs (e.g., paclitaxel, 23 ellipticine, 24,25 curcumin, 26 etc.) have been attempted to be released by (RADA) 4 or other similar ioncomplementary self-assembling peptides (e.g., EAK16-IV, EAK16-II and EFK-II, 24,27−29 MAX8, 30,31 etc.).…”
Section: Introductionmentioning
confidence: 99%
“…emission fluorescence peaks at about 390-440 nm, 468 nm, and 520 nm, respectively. 27 In the current study, the focus is on EAK-EPT complexes, where ellipticine was in a protonated state and is considered as green fluorescence. Both the flow cytometry and fluorescence microscopy used here were capable of detecting green fluorescence emitted by ellipticine at 520 nm.…”
Section: Antiproliferation Induced By Eak-ept Complexes Against A549 mentioning
confidence: 99%
“…The higher pH may lead to deprotonation of ellipticine and accordingly a lower zeta potential. 27 To study the interaction between EAK-EPT and plasma proteins under physiological conditions, the EAK-EPT complexes were incubated in bovine albumin serum, which is the most abundant protein in plasma. Over time, the zeta potential of EAK-EPT preincubated with bovine albumin serum decreased to -0.51 ± 0.08 mV with a stable particle size of ,100 nm.…”
Section: Nanostructure Of Eak-ept Complexesmentioning
confidence: 99%
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“…To gain a deeper understanding of the factors controlling the excited state relaxation processes, the fluorescent behavior of E was examined in organic solvents of a wide range of polarities and hydrogen bonding capabilities [3]. Selfassembling peptides was found to stabilize this alkaloid in water [4,5]. The native fluorescence of E and its protonated form (EH + ) was exploited to monitor their uptake and intracellular distribution [6,7].…”
Section: Introductionmentioning
confidence: 99%