Abstract
The promising applications of collagen in tissue engineering, regenerative medicine and biomaterials have intrigued great interest in development of collagen mimetic peptides (CMPs). In past decades, the large-scale collagen structures via the self-assembly of small CMPs have been extensively explored. Moreover, CMPs entail novel strategies in order to play a critical role in the discovery of new generation biomaterials. In this regard, we herein have synthesized a CMP, (Pro-Hyp-Gly)10 i.e. POG10. CMP has been examined in the presence of varying concentration of choline chloride (ChCl) by using various biophysical techniques such as circular dichroism (CD), UV–vis spectroscopy, fluorescence spectroscopy, Fourier transform infrared spectroscopy (FTIR) spectroscopy, differential scanning calorimetry (DSC), transmission electron microscopy (TEM) and dynamic light scattering (DLS). For the first time, we have demonstrated the use of choline chloride (ChCl) to manipulate stability and aggregation of CMP triple helices in order to delineate the factors responsible for the stability of triple helices.
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