Fig. 7
Characterizing collagen type I, derived from rat tail. (a) Freeze-dried collagen; (b) the collagen solution, pre-crosslinking at a concentration of 3 mg/mL; (c) self-assembled collagen under pH 7.4 and 37 °C conditions; (d) The FTIR spectrum indicating specific molecular vibrations such as amide A, amide B, amide I, amide II, and amide III, confirming the presence of the type 1 collagen structure; (e) SDS-PAGE data revealed collagen type 1 with two α1 chains and one α2 chain, as well as a β-dimer, further confirming the structure of collagen type I.
