摘要
Collagen mimetic peptides (CMPs) have garnered substantial interest in the field of regenerative medicine, tissue engineering, and biomaterials owing to their promising prospects for utilization within these domains. In the last few years, significant research efforts have been made to study how small CMPs can autonomously arrange themselves to create large scale collagen-like formations. These structures exhibit potential for advancing the field of next-generation biomaterials. In this investigation, we have synthesized a peptide named G-POG8, with the sequence Gly-Gly-(Pro-Hyp-Gly)8-Gly-Gly, and we have examined the behaviour of G-POG8 under different concentrations of choline chloride (ChCl) through various biophysical techniques. These methodologies include circular dichroism (CD), UV–vis, fluorescence and Fourier transform infrared (FTIR) spectroscopy, differential scanning calorimetry (DSC) transmission electron microscopy (TEM), and dynamic light scattering (DLS). The findings indicate that the presence of Gly at both terminals of the CMP, G-POG8, results in a significant influence on the stability and aggregation behaviour of CMP triple helices. It is plausible that ChCl may have established favourable interactions with the terminal residues of G-POG8, potentially disrupting the end-to-end process of triple helix aggregation. This investigation lays the basis for the development of innovative biomaterials based on collagen, featuring improved properties, and opens up possibilities for cutting-edge biomedical applications. © 2024 Elsevier B.V.