Nano Archive

The role of protecting groups in the formation of organogels through a nano-fibrillar network formed by self-assembling terminally protected tripeptides

Das, Apurba K. and Bose, Partha Pratim and Drew, Michael G. B. and Banerjee, Arindam (2007) The role of protecting groups in the formation of organogels through a nano-fibrillar network formed by self-assembling terminally protected tripeptides. Tetrahedron, 63 (31). 7432 - 7442.

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Official URL: http://www.sciencedirect.com/science/article/B6THR...

Abstract

A series of eight synthetic self-assembling terminally blocked tripeptides have been studied for gelation. Some of them form gels in various aromatic solvents including benzene, toluene, xylene, and chlorobenzene. It has been found that the protecting groups play an important role in the formation of organogels. It has been observed that, if the C-terminal has been changed from methyl ester to ethyl ester the gelation property does not change significantly (keeping the N-terminal protecting group same), while the change of the protecting group from ethyl ester to isopropyl ester completely abolishes the gelation property. Similarly, keeping the identical C-terminal protecting group (methyl ester) the results of the gelation study indicate that the substitution of N-terminal protection Boc- (tert-butyloxycarbonyl) to Cbz- (benzyloxycarbonyl) does change the gelation property insignificantly, while the change from Boc- to pivaloyl (Piv-) or acetyl (Ac-) group completely eliminates the gelation property. Morphological studies of the dried gels of two of the peptides indicate the presence of an entangled nano-fibrillar network that might be responsible for gelation. FTIR studies of the gels demonstrate that an intermolecular hydrogen bonding network is formed during gelation. Results of X-ray powder diffraction studies for these gelator peptides in different states (dried gels, gel, and bulk solids) reflected that the structure in the wet gel is distinctly different from the dried gel and solid state structures. Single crystal X-ray diffraction studies of a non-gelator peptide, which is structurally similar to the gelator molecules reveal that the peptide forms an antiparallel β-sheet structure in crystals.

Item Type:Article
Additional Information:Low Molecular Weight Organic Gelators
Uncontrolled Keywords:Organogelator; Nano-fibrillar; Self-assembly; Synthetic peptide
Subjects:Material Science > Nanofabrication processes and tools
Biomedical Science > Nanomedicine
ID Code:5713
Deposited By:SPI
Deposited On:27 Jul 2009 10:40
Last Modified:27 Jul 2009 10:40

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