Article
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Preserved in Portico This version is not peer-reviewed
Site-Specific Labeling of Proteins with Near-IR Dyes
Version 1
: Received: 19 October 2018 / Approved: 22 October 2018 / Online: 22 October 2018 (05:54:24 CEST)
A peer-reviewed article of this Preprint also exists.
Lin, C.-M.; Usama, S.M.; Burgess, K. Site-Specific Labeling of Proteins with Near-IR Heptamethine Cyanine Dyes. Molecules 2018, 23, 2900. Lin, C.-M.; Usama, S.M.; Burgess, K. Site-Specific Labeling of Proteins with Near-IR Heptamethine Cyanine Dyes. Molecules 2018, 23, 2900.
Abstract
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.
Keywords
heptamethine cyanine; protein labeling; thiol labeling; cancer targeting; vimentin
Subject
Chemistry and Materials Science, Organic Chemistry
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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