Interaction study of collagen and sericin in blending solution

Area of Science:

• Biomaterials Science
• Protein Chemistry
• Spectroscopy

Background:

• Collagen is a crucial structural protein with applications in tissue engineering and biomaterials.
• Sericin, a byproduct of silk processing, possesses biocompatibility and biodegradability.
• Understanding collagen-sericin interactions is key to developing novel biomaterials.

Purpose of the Study:

• To investigate the molecular interactions between collagen and sericin.
• To elucidate the structural and aggregation changes of collagen upon sericin addition.
• To evaluate the effect of sericin on the thermal stability of collagen.

Main Methods:

• Fluorescence spectroscopy
• Ultraviolet-visible spectroscopy
• Fourier-transform infrared (FTIR) spectroscopy, including 2D-FTIR
• Dynamic light scattering (DLS)
• Differential scanning calorimetry (DSC)

Main Results:

• Spectroscopic analyses indicated overlapping tyrosine residues between collagen and sericin, forming excimers and reducing collagen's hydrophobicity.
• FTIR and 2D-FTIR revealed weakened hydrogen bonds and alterations in collagen's triple helix structure in the presence of sericin.
• DLS showed a shift from pure collagen aggregates to hybrid collagen-sericin aggregates, with increasing size correlating to sericin content up to 60%.
• DSC confirmed that sericin enhances the thermal stability of collagen.

Conclusions:

• Sericin interacts with collagen at the molecular level, affecting its structure, aggregation, and hydrophobicity.
• The collagen-sericin complex exhibits increased thermal stability and altered aggregate formation.
• These findings suggest potential for collagen-sericin composites in advanced biomaterial applications.