Investigating the Role of Anion-π Interactions in the Cohesion of Peptidomimetic Polyether
발표자
이승현 (울산과학기술원)
연구책임자
이동욱 (울산과학기술원)
초록
내용
Anion-π interactions play a crucial role in biological processes, including ion transport and enzyme catalysis. Despite their importance, these interactions have been rarely investigated in synthetic polymer systems. This study explores anion-π interactions with chemically well-defined peptidomimetics, inspired by the molecular composition of mussel foot proteins. Two functional epoxide monomers–catechol acetonide glycidyl ether and 4,4-dimethy-2-oxazoline glycidyl ether–were employed to construct polyether-based polymers mimicking two crucial amino acids 3,4-dihydroxyphenylalanine and aspartic acid, respectively. The anion-π interactions between the polymers were analyzed using a surface forces apparatus with attention to the effects of pH and relative monomer composition. At an equimolar monomer ratio and neutral pH 7, the maximum cohesion energy of 15.0 mJ/m2 was observed. These findings highlight the potential of anion-π interactions to enhance the cohesive properties of synthetic polymers.