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Formation of Vesicles Through Solvent Assisted Self-Assembly of Hydrophobic Pentapeptides: Encapsulation and pH Responsive Release of Dyes by the Vesicles (Supplementary Mterial)

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In the biomimetic design two hydrophobic pentapetides Boc-Ile-Aib-Leu-Phe-Ala-OMe (I) and Boc-Gly-Ile- Aib-Leu-Phe-OMe (II) (Aib: α-aminoisobutyric acid) containing one Aib each are found to undergo solvent assisted selfassembly in methanol/water to form vesicular structures, which can be disrupted by simple addition of acid. The nanovesicles are found to encapsulate dye molecules that can be released by the addition of acid as confirmed by fluorescence microscopy and UV studies. The influence of solvent polarity on the morphology of the materials generated from the peptides has been examined systematically, and shows that fibrillar structures are formed in less polar chloroform/petroleum ether mixture and vesicular structures are formed in more polar methanol/water. Single crystal X-ray diffraction studies reveal that while β-sheet mediated self-assembly leads to the formation of fibrillar structures, the solvated β-sheet structure leads to the formation of vesicular structures. The results demonstrate that even hydrophobic peptides can generate vesicular structures from polar solvent which may be employed in model studies of complex biological phenomena.

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Keywords: DTA; Dynamic Light Scattering; Encapsulation; FT-IR Spectroscopy; Fibrils; N, N' dicyclohexylcarbodiimide; Single-Crystal X-Ray Diffraction; Thermo Gravimetric Analysis; UV-study; X-ray crystallography; X-ray diffraction; fluorescence; hydrophobic interactions; hydrophobic pentapeptides; hydrophobic peptides; lumenal vesicles; organogels; peptides; polarity; polydispersity index; self-assembly; vesicles

Document Type: Research Article

Publication date: September 1, 2011

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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