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Rapid Formation of Intramolecular Disulfide Bridges using Light: An Efficient Method to Control the Conformation and Function of Bioactive Peptides

Disulfide bonds are widely found in natural peptides and play a pivotal role in stabilizing their secondary structures, which are highly associated with their biological functions. Herein, we introduce a light-mediated strategy to effectively control the formation of disulfides. Our strategy is based on 2-nitroveratryl (oNv), a widely used photolabile motif, which serves both as a photocaging group and an oxidant (after photolysis). We demonstrated that irradiation of oNv-caged thiols with UV light could release free thiols that are rapidly oxidized by locally released byproduct nitrosoarene, leading to a "break-to-bond" fashion. This strategy is highlighted by the in situ restoration of the antimicrobial peptide tachyplesin I (TPI) from its external disulfide-caged analogue TPI-1. TPI-1 exhibits a distorted structure and a diminished function. However, upon irradiation, the β-hairpin structure and membrane activity of TPI were largely restored via rapid intramolecular disulfide formation. Our study proposes a powerful method to regulate the conformation and function of peptides in a spatiotemporal manner, which has significant potential for the design of disulfide-centered light-responsive systems.

 

Comments:

That's a fascinating strategy! Using light to control the formation of disulfide bonds in peptides presents exciting possibilities for regulating their structure and function. The ability to switch between different conformations or activities of peptides by manipulating disulfide bonds could have significant implications in various fields, including drug delivery, biotechnology, and materials science.

This method seems particularly promising for peptides like tachyplesin I (TPI), where the restoration of its native structure and function from a modified, disulfide-caged form (TPI-1) can be achieved through light-triggered disulfide bond formation. Being able to precisely modulate the structure and biological activity of peptides could lead to the development of tailored therapeutic agents or biomaterials with controlled functionalities.

The spatiotemporal control offered by light-mediated strategies allows for precise activation in specific locations at desired times, offering potential applications in targeted therapies or the development of smart materials responsive to environmental cues.

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S6570 TPI-1 TPI-1 (Tyrosine Phosphatase Inhibitor 1) is a potent inhibitor of SHP-1 with IC50 of 40 nM for recombinant SHP-1. TPI-1 exhibits anticancer activity.

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