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Self-Assembly of Recombinant Amphiphilic Oligopeptides into Vesicles

Self-Assembly of Recombinant Amphiphilic Oligopeptides into Vesicles,10.1021/bm0704267,Biomacromolecules,Albert J. van Hell,Cristina I. C. A. Costa,Fr

Self-Assembly of Recombinant Amphiphilic Oligopeptides into Vesicles   (Citations: 9)
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The aim of the present study was to design amphiphilic oligopeptides that can self-assemble into vesicular structures. The ratio of hydrophilic to hydrophobic block length was varied, and peptides were designed to have a hydrophobic tail in which the bulkiness of the amino acid side groups increases toward the hydrophilic domain (Ac-Ala- Ala-Val-Val-Leu-Leu-Leu-Trp-Glu2/7-COOH). These peptides were recombinantly produced in bacteria as an alternative to solid-phase synthesis. We demonstrate with different complementary techniques (dynamic and static light scattering, tryptophan fluorescence anisotropy, and electron microscopy) that these amphiphilic peptides spontaneously form vesicles with a radius of approximately 60 nm and a low polydispersity when dispersed in aqueous solution at neutral pH. Morphology and size of the vesicles were relatively insensitive to the variations in hydrophilic block length. Exposure to acidic pH resulted in formation of visible aggregates, which could be fully reversed to vesicles upon pH neutralization. In addition, it was demonstrated that water-soluble molecules can be entrapped inside these peptide vesicles. Such peptide vesicles may find applications as biodegradable drug delivery systems with a pH-dependent release profile.
Journal: Biomacromolecules , vol. 8, no. 9, pp. 2753-2761, 2007
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    • ...Previously, we developed amphiphilic oligopeptides that assemble into nanosized vesicles (10)...
    • ...The supramolecular structure exists in equilibrium with oligopeptides in free form, displaying a critical aggregation concentration (CAC) of around 0.5 μM for the SA2 peptide (10,11)...
    • ...E. Coli BL21(DE3) cells were transformed with plasmids encoding the SUMO-peptide fusion protein, and expression and protein purification were performed as described before (10)...
    • ...Forty microliters of each fraction were analyzed for calcein fluorescence as previously described (10)...
    • ...Considering that thiols can function as an elegant and reversible route to stabilize the peptide assemblies (16), two (SA2C2) or three (SA2C3) cysteines were introduced in the hydrophobic domain (Table I). The cysteine-containing peptides fused to the small-ubiquitin modifying protein (SUMO) were recombinantly produced in E. coli as previously described (10)...
    • ...Representative micrographs of the crosslinked peptide assemblies are shown in Fig. 3. As can be seen in the micrographs, both SA2C2 and SA2C3 samples (oxidized) showed spherical structures similar to what we have previously observed for SA2 peptides, which formed vesicles (10)...
    • ...After coating of the mica with polyornithine (10), the negatively charged peptide assemblies were immobilized on the surface, and AFM was performed in solution...
    • ...We have previously shown that non-crosslinked SA2 peptide vesicles can be loaded with calcein (10)...

    Albert J. van Hellet al. Stabilization of Peptide Vesicles by Introducing Inter-Peptide Disulfi...

    • ...Guo et al. [20] and Zhao et al. [21] Seddon and Templer [28] and Master et al. [29] Torchilin [30], Oku and Ishii [31], Fadel et al. [32], and de Leeuw et al. [33] van Hell et al. [34, 35] Wieder et al. [36] 17 The Future of Photodynamic Therapy 185...
    • ...A group of scientists have shown that recombinantly produced amphiphilic oligopeptides with amino acid sequence Ac-Ala-Ala-Val-Val-Leu-Leu-Leu-Trp-Glu-Glu spontaneously assemble into nano-sized vesicles with an average diameter of 120 nm [34]...

    Macrene Alexiades-Armenakas. The Future of Photodynamic Therapy

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