A designed amphiphilic peptide containing the silk fibroin motif as a potential carrier of hydrophobic drugs
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Zhou-2009-A designed amphiphil.pdf
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Author(s)
Zhou, Qinghan
Lin, Juan
Wang, Jing
Li, Feng
Tang, Fushan
Zhao, Xiaojun
Date Issued
November 2009
Journal
Progress in Natural Science
Publisher
Elsevier B.V.
Citation
Zhou, Qinghan, Juan Lin, Jing Wang, Feng Li, Fushan Tang, and Xiaojun Zhao. “A Designed Amphiphilic Peptide Containing the Silk Fibroin Motif as a Potential Carrier of Hydrophobic Drugs.” Progress in Natural Science 19, no. 11 (November 2009): 1529–1536.
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Final published version
Abstract
The amphiphilic peptide is becoming attractive as a potential drug carrier to improve the dissolvability of hydrophobic drugs in an aqueous system; thus, facilitating drug uptake by target cells. Here, we report a novel designed amphiphilic peptide, Ac-RADAGAGARADAGAGA-NH2, which was able to stabilize pyrene, a hydrophobic model drug we chose to study in aqueous solution. This designed peptide formed a colloidal suspension by encapsulating pyrene inside the peptide–pyrene complex. Egg phosphatidylcholine (EPC) vesicles were used to mimic cell bilayer membranes. We found that pyrene was released from the peptide coating into the EPC vesicles by mixing the colloidal suspension with EPC vesicles, which was followed by steady fluorescence spectra as a function of time. A calibration curve for the amount of pyrene released into the EPC vesicles at a given time was used to determine the final concentration of pyrene released into the lipid vesicles from the peptide–pyrene complex. The release rate of the peptide–pyrene complex was calculated to quantify the transfer of pyrene into EPC vesicles.
MIT Department
Massachusetts Institute of Technology. Center for Biomedical Engineering
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DOI of Published Version
https://doi.org/10.1016/j.pnsc.2009.04.010
