Design of protein homocystamides with enhanced tumor uptake properties for 19F magnetic resonance imaging

Chubarov, Alexey S.; Zakharova, Olga D.; Koval, Olga; Romaschenko, A. G.; Akulov, Andrey E.; Zavjalov, Evgenii L.; Разумов, И. А.; Koptyug, Igor V.; Knorre, D.G.; Godovikova, Tatyana S.

doi:10.1016/j.bmc.2015.09.043

Cited by 32 publications

(68 citation statements)

References 72 publications

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“…Spin labeling of HSA at Cys34 is successful with a wide range of spin label reagents based on several bioconjugate reactions . We chose methanethiosulfonate chemistry for the labels 4 , 10 , 17 , and 18 because of its typically high specificity in SDSL for free ‐SH groups .…”

Section: Resultssupporting

confidence: 84%

“…Modification by attachment of a spin label is no exception: we can think of a spin‐labeled cysteine as like a mutation to an unnatural amino acid. We consider this possible effect a potential concern, because modifications of HSA are well known to tune the physical properties and physiological functions of HSA . Therefore, we tested for aggregation of HSA and other gross changes using a gel retardation assay.…”

Section: Resultsmentioning

confidence: 99%

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Methanethiosulfonate Derivative of OX063 Trityl: A Promising and Efficient Reagent for Side‐Directed Spin Labeling of Proteins

Tormyshev

Chubarov

Krumkacheva

et al. 2020

Chemistry A European J

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Trityl radicals (TAMs) have recently appeared as an alternative source of spin labels for measuring long distances in biological systems. Finland trityl radical (FTAM) served as the basis for this new generation of spin labels, but FTAM is rather lipophilic and susceptible to self‐aggregation, noncovalent binding with lipophilic sites of proteins, and noncovalent docking at the termini of duplex DNA. In this paper the very hydrophilic OX063 TAM with very low toxicity and little tendency for aggregation is used as the basis for a spin label. Human serum albumin (HSA) labeled with OX063 has an intense narrow line typical of TAM radicals in solution, whereas HSA labeled with FTAM shows broad lines and extensive aggregation. In pulse EPR measurements, the measured phase memory time TM for HSA labeled with OX063 is 6.3 μs at 50 K, the longest yet obtained with a TAM‐based spin label. The lowered lipophilicity also decreases side products in the labeling reaction.

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Section: Resultssupporting

confidence: 84%

Section: Resultsmentioning

confidence: 99%

Methanethiosulfonate Derivative of OX063 Trityl: A Promising and Efficient Reagent for Side‐Directed Spin Labeling of Proteins

Tormyshev

Chubarov

Krumkacheva

et al. 2020

Chemistry A European J

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“…Electrophilic reactions to attach a nitroxide to the HTL amino group face the difficulty that the hydrochloride of HTL is chemically stable in bulk [46]. Attempts to obtain the free base for reaction results in the self-condensation of two HTL molecules [47,48]. The intrinsic instability of the HTL free Electrophilic reactions to attach a nitroxide to the HTL amino group face the difficulty that the hydrochloride of HTL is chemically stable in bulk [46].…”

Section: Synthesis Of N-substituted Homocysteine Thiolactone Derivativesmentioning

confidence: 99%

“…The intrinsic instability of the HTL free Electrophilic reactions to attach a nitroxide to the HTL amino group face the difficulty that the hydrochloride of HTL is chemically stable in bulk [46]. Attempts to obtain the free base for reaction results in the self-condensation of two HTL molecules [47,48]. The intrinsic instability of the HTL free base requires an electrophile with enhanced reactivity for efficient reaction with the amino group; examples include acid halides, activated carboxylic acids and anhydrides [39,49,50].…”

Section: Synthesis Of N-substituted Homocysteine Thiolactone Derivativesmentioning

confidence: 99%

Human Serum Albumin Labelled with Sterically-Hindered Nitroxides as Potential MRI Contrast Agents

et al. 2020

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Four albumin-nitroxide conjugates were prepared and tested as metal-free organic radical contrast agents (ORCAs) for magnetic resonance imaging (MRI). Each human serum albumin (HSA) carrier bears multiple nitroxides conjugated via homocysteine thiolactones. These molecular conjugates retain important physical and biological properties of their HSA component, and the resistance of their nitroxide groups to bioreduction was retained or enhanced. The relaxivities are similar for these four conjugates and are much greater than those of their individual components: the HSA or the small nitroxide molecules. This new family of conjugates has excellent prospects for optimization as ORCAs.

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“…Ранее [6], нами был разработан подход к декориро-ванию альбумина разным типом меток. В настоящей работе с его использованием был получен конъюгат альбумина PFT-Hcy-HSA-Cy7, содержащий магнит-но-резонансную метку (остаток перфтортолуола) и флуоресцентный краситель Cy7 (рис.…”

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Molecular Probes Based on the Human Serum Albumin for Tumor Visualization by Methods of Magnetic Resonance and Fluorescence Tomography

Chubarov¹,

Akulov²,

Shevelyov³

et al. 2016

SMR

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Design of protein homocystamides with enhanced tumor uptake properties for 19F magnetic resonance imaging

Cited by 32 publications

References 72 publications

Methanethiosulfonate Derivative of OX063 Trityl: A Promising and Efficient Reagent for Side‐Directed Spin Labeling of Proteins

Methanethiosulfonate Derivative of OX063 Trityl: A Promising and Efficient Reagent for Side‐Directed Spin Labeling of Proteins

Human Serum Albumin Labelled with Sterically-Hindered Nitroxides as Potential MRI Contrast Agents

Molecular Probes Based on the Human Serum Albumin for Tumor Visualization by Methods of Magnetic Resonance and Fluorescence Tomography

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