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  4. The Amphiphilic Self-Assembling Peptide EAK16-I as a Potential Hydrophobic Drug Carrier

The Amphiphilic Self-Assembling Peptide EAK16-I as a Potential Hydrophobic Drug Carrier

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Author(s)
Wang, Jing
•
Tang, Fushan
•
Li, Feng
•
Lin, Juan
•
Zhang, Yinghui
•
Du, Linfang
•
Zhao, Xiaojun
Date Issued
2008
Journal
Journal of Nanomaterials
Publisher
Hindawi Publishing Corporation
Citation
Wang, Jing, Fushan Tang, Feng Li, Juan Lin, Yinghui Zhang, Linfang Du, and Xiaojun Zhao. “The Amphiphilic Self-Assembling Peptide EAK16-I as a Potential Hydrophobic Drug Carrier.” Journal of Nanomaterials 2008 (2008): 1–8.
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Final published version
Abstract
It is crucial for hydrophobic drugs to be dissolved and stabilized by carriers in aqueous systems and then to be delivered into target cells. An amphiphilic self-assembling peptide EAK16-I (Ac-AEAKAEAKAEAKAEAK-NH2) is reported here to be able to stabilize a model hydrophobic compound, pyrene, in aqueous solution, resulting in the formation of colloidal suspensions. Egg phosphatidylcholine (EPC) vesicles are used as plasma membranes mimic. Fluorescence data shows that the pyrene is presented in the crystalline form when stabilized by EAK16-I and molecularly migrates from its peptide encapsulations into the membrane bilayers of EPC vesicles when the suspension is mixed with EPC vesicles. Furthermore, the release rate can be controlled by changing peptide-to-pyrene ratio, and the higher ratios lead to the slower release rates due to a thicker encapsulation on the pyrene microcrystals. This demonstrates that EAK16-I, as a promising nanobiomaterial, has the potential to be a hydrophobic compounds carrier.
MIT Department
Massachusetts Institute of Technology. Center for Biomedical Engineering
Terms of Use
Creative Commons Attribution
http://creativecommons.org/licenses/by/2.0
Persistent DSpace Link
http://hdl.handle.net/1721.1/96234
DOI of Published Version
https://doi.org/10.1155/2008/516286
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