RESUMO
Three-dimensional assemblies formed by multi-biopolymers perform important biological functions by maintaining the vital activities of living organisms through biochemical reactions that occur at the interfaces of these structures. In this study, we investigated the mechanism of the continuous variation of the secondary structural contents of interfacial peptides induced by the fusion of hydrogels with different charges. The hydrogel fusion induced continuous pH changes at the interface through ionic diffusion from the hydrogel matrices, and the pH value increased rapidly during the early stage (0-200 min) of the fusion process. In addition, the secondary structural content of the interfacial peptides changed continuously between the ß-sheet and random coil conformations during the early stage of the fusion process. The continuous variation in the secondary structural contents of the interfacial peptides was caused by (1) the protonation of peptide molecule amino acid side-chains in the region of pH change and (2) charge shielding due to the electrostatic interactions between the intramolecular peptides, intermolecular peptides, and intramolecular and intermolecular peptides.
