Supramolecular assembly of lysine-b-glycine block copolypeptides at different solution conditions

Jeffery Gaspard, James A. Silas, Daniel F. Shantz, Jeng Shiung Jan

Research output: Contribution to journalArticlepeer-review

39 Citations (Scopus)


Here we report the supramolecular assembly of poly(l-lysine)-b-polyglycine diblock copolypeptides at different solution conditions. Light scattering and confocal microscopy indicate that the supramolecular aggregates initially formed in solution are vesicles with a broad size distribution, depending strongly on the initial processing conditions. The vesicles formed after multiple pH cycles appear independent of the initial processing conditions and are related to the thermodynamic nature of the assembled supramolecular aggregates. Circular dichroism results verify that this change in size observed over pH cyclings tracks with the conformation changes of the lysine block confined in the vesicle membranes. This appears interesting for peptosome-based materials, implying a high level of fluidity in the membrane that allows the supramolecular aggregates formed in solution to respond to changes in pH. The results also show that the external stimulus, which is the change of pH in this study, provides an additional means to regulate polypeptide vesicle size and size distribution.

Original languageEnglish
Pages (from-to)178-185
Number of pages8
JournalSupramolecular Chemistry
Issue number3
Publication statusPublished - 2010 Mar

All Science Journal Classification (ASJC) codes

  • Chemistry(all)


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