Self-assembled micelles of a multi-functional amphiphilic fusion (MFAF) peptide for targeted cancer therapy

Yin Jia Cheng, Hong Cheng, Xin Zhao, Xiao Ding Xu, Ren Xi Zhuo, Feng He

Research output: Journal article publicationJournal articleAcademic researchpeer-review

11 Citations (Scopus)


A new multi-functional amphiphilic fusion (MFAF) peptide comprised of a multi-functional fusion peptide sequence (GFLGR8GDS) and a hydrophobic polycaprolactone (PCL) tail was designed and prepared. In aqueous solution, through the strong hydrophobic interaction among the PCL tails, this MFAF peptide can self-assemble into core-shell micelles at a low concentration with the anti-tumor drug doxorubicin (DOX) loaded in the core and the multi-functional fusion peptide sequence located on the shell. When incubating the DOX-loaded micelles with tumor and normal cells, the micelles can use the RGD and membrane-penetrating peptide (eight continuous arginine residues, R8) sequences to target tumor cells and penetrate cell membranes. Subsequently, cathepsin B, an enzyme over-expressed in late endosomes and lysosomes of tumor cells that can specifically hydrolyze the GFLG sequence, can break the micellar structure and lead to a rapid release and escape of loaded DOX from endosomes, resulting in the apoptosis of tumor cells. The MFAF peptide presents great potential as a new drug delivery platform for targeted cancer chemotherapy. This journal is
Original languageEnglish
Pages (from-to)3512-3520
Number of pages9
JournalPolymer Chemistry
Issue number18
Publication statusPublished - 14 May 2015
Externally publishedYes

ASJC Scopus subject areas

  • Bioengineering
  • Biochemistry
  • Polymers and Plastics
  • Organic Chemistry


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