Probing the intermolecular interactions and local environments of self-assembled peptide nanostructures (SPNs) is crucial for a better understanding of the underlying molecular details of self-assembling phenomena. In particular, investigation of the hydration state is important to understand the nanoscale structural and functional characteristics of SPNs. In this report, we examined the local hydration environments of SPNs in detail to understand the driving force of the discrete geometric structural self-assembling phenomena for peptide nanostructures. Advanced electron paramagnetic resonance spectroscopy was used to probe the hydrogen bond formation and geometry as well as the hydrophobicity of the local environments at various spin-labeled sites in SPNs. The experimental results supplement the sparse experimental data regarding local structures of SPNs, such as the hydrogen bonding and the hydrophobicity of the local environment, providing important information on the formation of SPNs, which have immense potential for bioactive materials.
Bibliographical noteFunding Information:
This work was supported by grants from the National Research Foundation (NRF) of Korea (2017R1A2B4008691 and 2017M3D1A1039380 to S.H.K. and 2017R1A2A2A05069773 to Y.B.L.).
© 2019 American Chemical Society.
All Science Journal Classification (ASJC) codes
- Chemical Engineering(all)