Abstract

Targeted chemical modification of peptides and proteins by laser pulses in a biologically relevant environment, i.e. aqueous solvent at room temperature, allows for accurate control of biological processes. However, the traditional laser methods of control of chemical reactions are applicable only to a small class of photosensitive biomolecules because of strong and ultrafast perturbations from biomolecule-solvent interactions. Here, we report excitation of harmonics of vibration modes of solvent molecules by femtosecond laser pulses to produce controlled chemical modifications of non-photosensitive peptides and proteins in polar liquids under room conditions. The principal modifications included lysine formylation and methionine sulfoxidation both of which occur with nearly 100% yield under atmospheric conditions. That modification occurred only if the laser irradiance exceeded certain threshold level. The threshold, type, and extent of the modifications were completely controlled by solvent composition, laser wavelength, and peak irradiance of ultrashort laser pulses. This approach is expected to assist in establishing rigorous control over a broad class of biological processes in cells and tissues at the molecular level.

Highlights

  • Femtosecond laser pulses are capable of precisely controlling the pathway and final products of numerous chemical modifications of organic and inorganic molecules[1,2,3,4]

  • We propose a method that builds a foundation for non-coherent control of biological functions by permanent laser-induced chemical modifications that

  • The results show that single formylation on primary amines was the predominant chemical modification produced by irradiation with femtosecond laser pulses at 386 nm (Fig. 4; Supplementary Fig. S32)

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Summary

Discussion

The data presented demonstrate that femtosecond laser pulses can produce formylation on primary amines of peptides and proteins. Since the energy of the 8th harmonic is close to the energy of bond breaking, this excitation creates a situation favorable for breaking the O-H bonding before any remarkable relaxation by energy transfer to other vibration modes This process can produce CH3O and H fragments in the liquid, the former fragment would produce formylation of the peptide in methanol which was not detected in our experiments. 100% modification of primary amines only suggests that corresponding biomolecule-solvent hydrogen bonds are the most effectively converted into internal biomolecule covalent bonding by proper laser excitation of interacting molecules This result demonstrates that the reported approach can be a universal method to produce a variety of laser-assisted biochemical synthesis reactions in polar liquids. Treatment of peptides and proteins with femtosecond laser pulses leads to a precise irreversible chemical modification of biomolecules in polar liquids enriched with dissolved air and potentially provides a means for well-defined optical control of biological processes at the molecular level

Materials and Methods
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