Abstract:
The design and development of an efficient biomaterial which is capable of
supporting growth of cells in 3D, is an important milestone for biomedical
applications. Self assembling peptide hydrogels are promising biomaterial owing to
their biocompatibility and biodegradability. Their physical and mechanical properties
can also be easily tailored. In the present study we designed two ionic complementary
hexapeptides that differ in hydrophobicity i.e., FK6 (FEFGFK) and VK6 (VEVGVK)
where F is phenylalanine, G is glycine, K is lysine, E is glutamic acid and V is valine.
The aim of this study was to investigate the effect of hydrophobicity, concentration,
pH and temperature on the gelation of these peptides. Morphological characterization
of the peptide hydrogels was performed by Fourier Transformed Infrared
Spectroscopy (FTIR) and Scanning Electron Microscopy (SEM) which revealed that
the peptides self assemble into beta sheet structures when in solution form. These beta
sheet structures align to form nanofibrils. Hydrogel formation for FK6 was observed at
a specific concentration with stability at optimum pH and temperature required for cell
culture, whereas, no gelation was observed in case of VK6 indicating a direct role of
hydrophobicity in the gel formation. The hemocompatibility of the designed peptide
hydrogels was also observed, where in FK6 showed barely any hemolysis of red blood
cells (RBCs). Therefore, the FK6 peptide hydrogel is proposed to be a promising
scaffold for various tissue engineering applications.
