Stabilization of peptide-based vesicles via in situ oxygen-mediated cross-linking

Adrian Sulistio, Anton Blencowe, Jiapei Wang, Gary Bryant, Xiaoqing Zhang, Greg Qiao

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24 Citations (Scopus)


Reversible vesicles from poly(L-glutamic acid)65-block-poly[(L-lysine)-ran-(L-3,4-dihydroxyphenylalanine)]75 [PLGA65-b-P(LL-r-DOPA)75] block copolypeptide adopt different configurations depending on the surrounding pH. At pH=3, AFM and TEM images show ellipsoidal morphologies, whereas at pH=12 both TEM and AFM reveal the formation of hollow vesicles. At pH=12, the P(LL-r-DOPA) block forms the internal layer of the vesicle shell and the subsequent oxygen-mediated oxidation of the phenolic groups of the DOPA lead to the formation of quinonic intermediates, which undergo intermolecular dimerization to stabilize the vesicles via in situ cross-linking. Consequently, the vesicles maintain their shape even when the pH is reversed back to 3, as confirmed by AFM and TEM.

Original languageEnglish
Pages (from-to)1220-1231
Number of pages12
JournalMacromolecular Bioscience
Issue number9
Publication statusPublished - Sep 2012
Externally publishedYes


  • Amino acid NCAs
  • Block copolypeptides
  • Cross-linking
  • Reversible
  • Vesicles

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