Modeling of adsorption dynamics at air–liquid interfaces using statistical rate theory (SRT)

Biswas, M.E.; Chatzis, Ioannis; Ioannidis, Marios A.; Chen, P.

doi:10.1016/j.jcis.2005.01.011

Cited by 11 publications

(1 citation statement)

References 34 publications

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“…Surface tension is a solution property and based on the molecular adsorption at the interface, affecting the surface free energy. The adsorption process involves three steps: i) diffusion of the molecules from the bulk to the sub-interface; ii) transfer of the molecules from the sub-interface to the interface; iii) rearrangement of the molecules at the interface [32]. Considering diffusion to be the rate limiting step, small molecules are expected to rapidly accumulate at the interface due to their faster diffusion rate than large ones.…”

Section: Resultsmentioning

confidence: 99%

Sequence Effect of Self-Assembling Peptides on the Complexation and In Vitro Delivery of the Hydrophobic Anticancer Drug Ellipticine

2008

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A special class of self-assembling peptides has been found to be capable of stabilizing the hydrophobic anticancer agent ellipticine in aqueous solution. Here we study the effect of peptide sequence on the complex formation and its anticancer activity in vitro. Three peptides, EAK16-II, EAK16-IV and EFK16-II, were selected to have either a different charge distribution (EAK16-II vs. EAK16-IV) or a varying hydrophobicity (EAK16-II vs. EFK16-II). Results on their complexation with ellipticine revealed that EAK16-II and EAK16-IV were able to stabilize protonated ellipticine or ellipticine microcrystals depending on the peptide concentration; EFK16-II could stabilize neutral ellipticine molecules and ellipticine microcrystals. These different molecular states of ellipticine were expected to affect ellipticine delivery. The anticancer activity of these complexes was tested against two cancer cell lines: A549 and MCF-7, and related to the cell viability. The viability results showed that the complexes with protonated ellipticine were effective in eradicating both cancer cells (viability <0.05), but their dilutions in water were not stable, leading to a fast decrease in their toxicity. In contrast, the complexes formulated with EFK16-II were relatively stable upon dilution, but their original toxicity was relatively low compared to that with protonated ellipticine. Overall, the charge distribution of the peptides seemed not to affect the complex formation and its therapeutic efficacy in vitro; however, the increase in hydrophobicity of the peptides significantly altered the state of stabilized ellipticine and increased the stability of the complexes. This work provides essential information for peptide sequence design in the development of self-assembling peptide-based delivery of hydrophobic anticancer drugs.

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Section: Resultsmentioning

confidence: 99%