Abstract
Gel-sol transition of peptides is useful for environment-dependent drug release. For the applications, kinetics control of the responses is important for matching the releasing velocity to the target events. We demonstrate a rational control of redox-triggered gel-sol transition kinetics of self-assembling peptides by the amino acid sequence. A sequence bearing a redox-active methionine (Met) residue near a terminus allowed for faster oxidation-triggered gel-sol transition with reactive oxygen species such as hydrogen peroxide than a peptide possessing a Met residue at the center. The present study contributes not only to the biomaterials design but also to the biological research on the kinetic effects of Met oxidation depending on its position in proteins on pathology. More information can be found in the Research Article by T. Muraoka et al.
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