生体分子で作る抗付着性表面

抄録

Biomolecules interact with their target molecules accurately in crowded conditions in cells or bodies with rarely making mistakes (non-specific binding). In this review, we discuss the mechanism underlying the accuracy in the molecular recognition of biomolecules, in particular, the suppression of non-specific interactions. Our surface force measurements revealed that water-mediated force critically governs the colloidal stability of Au nanoparticles covered with DNA molecules. The colloidal stability depended on the complementarity of the terminal base pairs. In the case of the peptide molecules, the SAMs of peptide that contains zwitterionic pairs of glutamic acids and lysines exhibited excellent anti-fouling properties, whereas the SAMs of peptide that possesses glutamic acids and arginines did not. We also found that interfacial water plays an essential role as a barrier preventing the approach of proteins and cells. From these findings, we are noticing that biomolecules smartly use their interfacial water to accomplish their specific interactions.