Ligand-directed dibromophenyl benzoate chemistry for rapid and selective acylation of intracellular natural proteins

Takaoka, Yousuke; Nishikawa, Yuki; Hashimoto, Yuki; Sasaki, Kenta; Hamachi, Itaru

doi:10.1039/c5sc00190k

Cited by 79 publications

(75 citation statements)

References 45 publications

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“…Hamachi and coworkers have successfully expanded the cleavable electrophile range, from tosyl (LDT) to acyl imidazole (LDAI) ( Fig. 16), 196 dibromophenyl benzoate (LDBB), 197 N-sulfonyl pyridone (LDSP) (Fig. 16i) 198 and N-acyl-N-alkyl-sulfonamide (LDNASA) (Fig.…”

Section: •2 Traceless Affinity-based Chemical Labeling Of Endogenousmentioning

confidence: 99%

Recent Progress in Chemical Modification of Proteins

Sakamoto

Hamachi

2018

ANAL. SCI.

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Chemical modification of proteins is important for creating a myriad of engineered proteins and for elucidating the function and dynamics of proteins in live cells. A wide variety of chemical protein modification methods have been developed and can be categorized into three classes: (i) modification of proteins using the reactivity of naturally occurring amino acids; (ii) modification by bioorthogonal reactions using unnatural amino acids, most of which can be siteselectively incorporated into proteins-of-interest using genetic codon expansion techniques; and (iii) recognition driven chemical modification, which is the only approach that allows modification of endogenous proteins without any genetic manipulation even under heavily crowded and multi-molecular conditions, as in live cells and organisms. All of these approaches have merits and limitations. In this review, we summarize these approaches and discuss their characteristics with respect to specificity, reaction rate and versatility.

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Section: •2 Traceless Affinity-based Chemical Labeling Of Endogenousmentioning

confidence: 99%

Recent Progress in Chemical Modification of Proteins

Sakamoto

Hamachi

2018

ANAL. SCI.

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“…A probe containing an acyl‐transferring moiety was developed using a dibromophenyl benzoate (Figure B) . The dibromo motif was found to have superior bioconjugation efficiency compared to both a single o ‐nitro‐ or dichloro‐modification of the phenol moiety.…”

Section: Reactive Moietymentioning

confidence: 99%

“…Ligand‐directed dibromophenyl benzoate probes were applied to labeling of different proteins with fluorophores or biotin in living cells . The conjugation showed high selectivity for the targeted proteins, but off‐labeling was also observed with BSA, which indicate that the probes may not be suitable for in vivo labeling.…”

Section: Reactive Moietymentioning

confidence: 99%

Considerations on Probe Design for Affinity‐Guided Protein Conjugation

2019

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The plethora of methods developed for the creation of protein conjugates often differs significantly with regard to the heterogeneity of the resulting products, in the degree of genetic manipulation of the protein required, and in the technical skills required to perform the conjugation procedure. Affinity‐guided protein conjugation is a protein labeling methodology based on noncovalent binding interactions between a labeling probe and the protein of interest. These interactions increase the local concentration of a reactive group in the probe on the protein surface thus facilitating the conjugation in proximity of the complexation site. The ability to produce high‐quality conjugates from nongenetically modified proteins both in vitro, but also in cells, demonstrates the power of affinity‐guided protein conjugation. Here, we present the progress of affinity‐guided protein conjugation in relation to selective protein labeling in living systems and the formation of high‐quality protein conjugates. Furthermore, the probe design will be discussed in relation to the utility of the probe for labeling in vitro or in living systems.

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“…[57][58][59] The labeling and chemicalmodifying technology, which are recently attracting much attention, are affinity-based labeling such as represented by ligand-directed tosyl chemistry developed by Hamachi and colleagues. [60][61][62] General design of this type of protein-labeling reagent is shown in Fig. 9A.…”

Section: Sealide-based Protein Labeling Reagent 331 Design Of Sealmentioning

confidence: 99%

Development of Chemical Biology Tools Focusing on Peptide/Amide Bond Cleavage Reaction

Shigenaga

2019

CHEMICAL & PHARMACEUTICAL BULLETIN

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Peptides and proteins are involved in almost all biological events. In this review, three chemical biology tools, which were developed for peptide/protein sciences from a viewpoint of peptide/amide bond cleavage, are overviewed. First, study on an artificial amino acid that enables stimulus-responsive functional control of peptides/proteins is briefly described. Two N-S acyl transfer reaction-based tools, one a linker molecule for facile identification of target proteins of bioactive compounds and the other a reagent for selective labeling of proteins of interest, are then discussed.

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Ligand-directed dibromophenyl benzoate chemistry for rapid and selective acylation of intracellular natural proteins

Abstract: A rapid and selective protein labeling method, LDBB chemistry is a useful tool for natural protein imaging in living cells.

Cited by 79 publications

References 45 publications

Recent Progress in Chemical Modification of Proteins

Recent Progress in Chemical Modification of Proteins

Considerations on Probe Design for Affinity‐Guided Protein Conjugation

Development of Chemical Biology Tools Focusing on Peptide/Amide Bond Cleavage Reaction

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