Reaction of diazonium salt with tyrosine residues in polypeptides

Pieroni, Osvaldo; Fissi, Adriano; Houben, Julien L.

doi:10.1002/macp.1975.021761106

Cited by 6 publications

(3 citation statements)

References 14 publications

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“…9 In fact, CD has been used as a method of choice to monitor the interconversion of a right-handed helix into a left-handed helix in a model dehydrophenylalanine containing peptide, as a function of change in solvent and temperature. 23 In ∆Phe containing peptides which adopt right-handed 3 10 -helical structures, very similar CD pattern have been observed; 9,21 the CD spectrum in most cases displays a couplet of intense bands with opposite signs (-+) at ∼300 nm and ∼270 nm and a crossover at ∼275-285 nm. This CD pattern is a typical exciton splitting…”

Section: Discussionmentioning

confidence: 73%

First Observation of Left-Handed Helical Conformation in a Dehydro Peptide Containing Two l-Val Residues. Crystal and Solution Structure of Boc-l-Val-ΔPhe-ΔPhe-ΔPhe-l-Val-OMe^,

et al. 1997

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The solution and solid structure of Boc-l-Val-ΔPhe-ΔPhe-ΔPhe-l-Val-OMe, containing three consecutive ΔPhe residues, have been determined by X-ray diffraction, nuclear magnetic resonance, and circular dichroism methods. The crystals grown from aqueous methanol are orthorhombic, space group P212121, a = 11.624(2), b = 17.248(2), c = 21.532 Å, V = 4216 (1) Å3, Z = 4. In the solid state, the peptide exhibits a left-handed 310-helical conformation, in spite of the presence of two l-Val residues. NMR and CD studies in different solvents also support the crystal structure data, suggesting that the solid state structure is maintained in solution as well. This is the first report of a dehydropeptide containing three consecutive ΔPhe residues and exhibiting left-handed 310-helical conformation, which demonstrates the remarkable conformational consequences produced by consecutive occurrence of ΔPhe residues in a peptide.

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Section: Discussionmentioning

confidence: 73%

First Observation of Left-Handed Helical Conformation in a Dehydro Peptide Containing Two l-Val Residues. Crystal and Solution Structure of Boc-l-Val-ΔPhe-ΔPhe-ΔPhe-l-Val-OMe^,

et al. 1997

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“…The modification of tyrosine with aryl diazonium ions via electrophilic aromatic substitution is one of the oldest selective bioconjugation strategies, and one that is still used in modern applications. [2, 3] An early concern was that azobenzenes are often found in fluorescent quencher motifs, [4] but upon investigation there are examples of azobenzene-coumarin compounds that have fluorescent properties. [5, 6] One example in particular that offered encouragement was a reported coumarin-derived aryl diazonium ion that acted as a covalent inhibitor of acetyl choline esterase which became fluorescent upon modification of tyrosine in the enzymatic pocket.…”

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confidence: 99%

Coumarin Triazabutadienes for Fluorescent Labeling of Proteins

et al. 2018

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The use of small-molecule fluorophores to label proteins with minimal perturbation in response to an external stimulus is a powerful tool to probe chemical and biochemical environments. Herein we describe first the use of a coumarin modified triazabutadiene that can deliver aryl diazonium ions to fluorescently label proteins via tyrosine selective modification. The labeling can be triggered by low pH induced liberation of the diazonium species, making the fluorophore specifically useful in labeling biochemical surroundings such as those found within the late endosome. Additionally, we show that a variety of coumarin triazabutadienes may also be prone to releasing their diazonium cargo via irradiation with UV light.

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“…Among the different Y bioconjugation reactions, we specifically focused on the diazo-coupling reaction. In this reaction, aryldiazonium salts, prepared from the corresponding aniline by the action of a nitrite in an acidic medium, establish an azo linkage with the phenol side ring of Y via electrophilic aromatic substitution [25] . We used two targeting ligands with a reactive diazonium salt coupling function to chemically modify the rAAV2 capsid (Figure 1).…”

Section: Resultsmentioning

confidence: 99%

Novel chemical tyrosine functionalization of adeno-associated virus improves gene transfer efficiency in liver and retina

Leray

Lalys

Varin

et al. 2023

Preprint

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Decades of biological and clinical research have led to important advances in recombinant adeno-associated viruses rAAV-based gene therapy gene therapy. However, several challenges must be overcome to fully exploit the potential of rAAV vectors. Innovative approaches to modify viral genome and capsid elements have been used to overcome issues such as unwanted immune responses and off-targeting. While often successful, genetic modification of capsids can drastically reduce vector yield and often fails to produce vectors with properties that translate across species. Here, we describe a chemical bioconjugation strategy to modify tyrosine residues on AAV capsids using specific ligands, thereby circumventing the need to genetically engineer the capsid sequence. Aromatic electrophilic substitution of the phenol ring of tyrosine residues on AAV capsids improved the in vivo transduction efficiency of rAAV2 vectors in both liver and retinal targets. This tyrosine bioconjugation strategy represents an innovative technology for the engineering of rAAV vectors for human gene therapy.

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Reaction of diazonium salt with tyrosine residues in polypeptides

Cited by 6 publications

References 14 publications

First Observation of Left-Handed Helical Conformation in a Dehydro Peptide Containing Two l-Val Residues. Crystal and Solution Structure of Boc-l-Val-ΔPhe-ΔPhe-ΔPhe-l-Val-OMe^,

First Observation of Left-Handed Helical Conformation in a Dehydro Peptide Containing Two l-Val Residues. Crystal and Solution Structure of Boc-l-Val-ΔPhe-ΔPhe-ΔPhe-l-Val-OMe^,

Coumarin Triazabutadienes for Fluorescent Labeling of Proteins

Novel chemical tyrosine functionalization of adeno-associated virus improves gene transfer efficiency in liver and retina

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Reaction of diazonium salt with tyrosine residues in polypeptides

Cited by 6 publications

References 14 publications

First Observation of Left-Handed Helical Conformation in a Dehydro Peptide Containing Two l-Val Residues. Crystal and Solution Structure of Boc-l-Val-ΔPhe-ΔPhe-ΔPhe-l-Val-OMe,

First Observation of Left-Handed Helical Conformation in a Dehydro Peptide Containing Two l-Val Residues. Crystal and Solution Structure of Boc-l-Val-ΔPhe-ΔPhe-ΔPhe-l-Val-OMe,

Coumarin Triazabutadienes for Fluorescent Labeling of Proteins

Novel chemical tyrosine functionalization of adeno-associated virus improves gene transfer efficiency in liver and retina

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Product

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First Observation of Left-Handed Helical Conformation in a Dehydro Peptide Containing Two l-Val Residues. Crystal and Solution Structure of Boc-l-Val-ΔPhe-ΔPhe-ΔPhe-l-Val-OMe^,

First Observation of Left-Handed Helical Conformation in a Dehydro Peptide Containing Two l-Val Residues. Crystal and Solution Structure of Boc-l-Val-ΔPhe-ΔPhe-ΔPhe-l-Val-OMe^,