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Stabilization of Peptide‐Based Vesicles via in situ Oxygen‐Mediated Cross‐Linking
Author(s) -
Sulistio Adrian,
Blencowe Anton,
Wang Jiapei,
Bryant Gary,
Zhang Xiaoqing,
Qiao Greg G.
Publication year - 2012
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.201200048
Subject(s) - vesicle , chemistry , in situ , biophysics , crystallography , lysine , stereochemistry , polymer chemistry , amino acid , membrane , organic chemistry , biochemistry , biology
Reversible vesicles from poly( L ‐glutamic acid) 65 ‐block‐ poly[( L ‐lysine)‐ ran ‐( L ‐3,4‐dihydroxyphenylalanine)] 75 [PLGA 65 ‐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.