Site-Specific Labeling of Proteins with Near-IR Dyes

Chen-Ming Lin; Syed Muhammad Usama; Kevin Burgess

doi:10.20944/preprints201810.0473.v1

Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Version 1 : Received: 19 October 2018 / Approved: 22 October 2018 / Online: 22 October 2018 (05:54:24 CEST)

Convenient labeling of proteins is important for observing its function under physiological conditions. In tissues particularly, heptamethine cyanine dyes (Cy-7) are valuable because they absorb in near infrared (NIR) region (750 – 900 nm) where light penetration is maximal. In this work, we found Cy-7 dyes with a meso-Cl functionality covalently binding to proteins with free Cys residues under physiological conditions (aqueous environments, at near neutral pH, and 37 °C). It transpired that the meso-Cl of the dye was displaced by free thiols in protein, while nucleophilic side-chains from amino acids like Tyr, Lys, and Ser did not react. This finding shows a new possibility for convenient and selective labeling of proteins with near-IR fluorescent probes.

heptamethine cyanine; protein labeling; thiol labeling; cancer targeting; vimentin

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Site-Specific Labeling of Proteins with Near-IR Dyes

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