Pentapeptide based organogels: the role of adjacently located phenylalanine residues in gel formation

Abstract

A terminally protected self-assembling pentapeptide Boc-Leu(1)-Val(2)-Phe(3)-Phe(4)-Ala(5)-OMe 1 bearing sequence similarity with Aβ^17–21 (the fragment 17–21 of the amyloid β-peptide Aβ⁴²) forms thermoreversible transparent gels in various organic solvents including benzene, toluene, m-xylene and 1,2-dichlorobenzene. A series of its variants have been synthesized in order to study the role of adjacently located phenylalanine residues and the protecting groups for gelation in different organic solvents. Replacement of any of the Phe residues of the Phe-Phe segment with any other hydrophobic α-amino acid residue drastically changes the gel forming properties indicating that both Phe residues have an important role in gel formation. These gels are characterised using field emission scaning electron microscopy (FE-SEM), transmission electron microscopy (TEM), FT-IR and wide angle X-ray scattering (WAXS) studies. WAXS studies of the peptide 1–benzene gel indicate that π–π interaction is responsible for gel formation and it reveals the necessity of the Phe residues in gel formation. Transmission electron microscopy (TEM) of the gels reveals a nanofibrillar morphology, which is obtained from the self-assembled gelators in the gel phase. These gels bind with a physiological dye, Congo red, and show a green birefringence under cross polarizers, which is a characteristic feature of amyloid fibrils.