Peptides with proper sequences are capable of self-assembling into well-defined nanostructures, which can subsequently grow and entangle into three-dimensional nanomatrices. In this study, hemopressin, a cannabinoid receptor-modulating peptide derived from the α-chain of hemoglobin known to self-assemble into nanofibrils, was examined for its potential applicability as a gelator. The results indicated that hemopressin's gel formation was dependent on pH and salt concentration. Although hemopressin's macroscopic states showed differences, its microscopic structure remained largely unchanged in which it consisted mainly of the antiparallel β-sheet conformation as confirmed by FTIR (C=O stretch peaks at 1630 and 1695 cm-1) and CD (β-sheet peak at 195 nm). The major difference between the gel and sol states was displayed in the fibril length in which the gelation at pH 7.4 resulted in 4 μm fibrils, whereas the solution at pH 5.0 showed 800 nm fibrils. The pH-dependent sol-gel phase transition property was then utilized for the investigation of the pH-responsive release of FITC-dextran (4-40 kDa) from hemopressin fibrillary gel. Finally, the biocompatibility of the peptide was demonstrated by proliferation assay of cultured bone marrow mesenchymal stem cells. Altogether, the results suggested that hemopressin is a potentially promising candidate as a therapeutically active platform for drug delivery.
Keywords: hemopressin; pH-sensitive; peptide hydrogel; self-assembly; β-sheet.