Continuous Variation of Secondary Structural Contents of Interfacial Peptides Induced by Hydrogel Fusion

Area of Science:

• Biochemistry
• Materials Science
• Biophysics

Background:

• Multi-biopolymer assemblies are vital for biological functions.
• Biochemical reactions occur at the interfaces of these structures.
• Understanding interfacial peptide behavior is key to biological processes.

Purpose of the Study:

• To investigate how fusing hydrogels with different charges affects interfacial peptide secondary structures.
• To elucidate the mechanism behind continuous structural variations in peptides at hydrogel interfaces.

Main Methods:

• Fusion of hydrogels with differing charges.
• Monitoring pH changes at the interface via ionic diffusion.
• Analyzing secondary structural content of interfacial peptides (e.g., beta-sheet, random coil).

Main Results:

• Hydrogel fusion induced continuous pH changes at the interface, with rapid increase in the early stage (0-200 min).
• Interfacial peptide secondary structures continuously varied between beta-sheet and random coil conformations during this period.
• Structural changes were attributed to pH-induced amino acid side-chain protonation and electrostatic charge shielding.

Conclusions:

• Hydrogel fusion dynamically alters interfacial environments, specifically pH.
• This dynamic pH change directly influences peptide secondary structures.
• The findings provide insights into the structure-function relationship of biopolymer assemblies in biological systems.