Seleno l methionine

Manufactured by Nacalai Tesque

Sourced in Japan

Seleno-l-methionine is a selenium-containing amino acid. It is used as a precursor for the synthesis of selenoproteins in biological systems.

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Lab products found in correlation

Odium selenate, by Fujifilm (2 mentions) L selenocystine secys2, by Thermo Fisher Scientific (2 mentions) Sodium selenite, by Nacalai Tesque (2 mentions) Se methylseleno l cysteine mesecys, by Thermo Fisher Scientific (2 mentions)

3 protocols using seleno l methionine

Bioselenocompounds: Structural Diversity and Biological Significance

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Sodium selenate and potassium selenocyanate (SeCN⁻) were purchased from Wako Pure Chemical Industries, Ltd. (Osaka, Japan). Sodium selenite and seleno-l-methionine (SeMet) were purchased from Nacalai Tesque (Kyoto, Japan). Se-Methylseleno-l-cysteine (MeSeCys) and l-selenocystine (SeCys₂) were purchased from Acros Organics (Waltham, MA) and Tokyo Chemical Industry Co., Ltd. (Tokyo, Japan), respectively. Trimethylselenonium iodide (TMSe⁺) was purchased from Tri Chemical (Uenohara, Japan). l-Selenohomolanthionine (SeHLan) and 1β-methylseleno-N-acetylgalactosamine (SeSug1) were synthesized in our laboratory in accordance with our previous work [7 ,8 (link)]. The chemical structures of the bioselenocompounds used in this study are shown in Fig. 1.Fig. 1

Structures of bioselenocompounds used in this study. SeCN⁻: selenocyanate, SeMet: selenomethionine, MeSeCys: Se-methylselenocysteine, SeHLan: selenohomolanthionine, SeCys₂: selenocystine, SeSug1: 1β-methylseleno-N-acetylgalactosamine, TMSe⁺: trimethylselenonium ion.

Fig. 1

Kobayashi H., Suzuki N, & Ogra Y. (2018). Mutagenicity comparison of nine bioselenocompounds in three Salmonella typhimurium strains. Toxicology Reports, 5, 220-223.

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Synthesis of Selenocompounds for Biological Study

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Sodium selenate and potassium selenocyanate (SeCN⁻) were purchased from Wako Pure Chemical Industries, Ltd. (Osaka, Japan). Sodium selenite and seleno-l-methionine (SeMet) were purchased from Nacalai Tesque (Kyoto, Japan). Se-Methylseleno-l-cysteine (MeSeCys) and l-selenocystine (SeCys₂) were purchased from Acros Organics (Waltham, MA, USA) and Tokyo Chemical Industry Co., Ltd. (Tokyo, Japan), respectively. Trimethylselenonium iodide (TMSe⁺) was purchased from Tri Chemical (Uenohara, Japan). l-Selenohomolanthionine (SeHLan) and Se-methylseleno-N-acetylgalactosamine (SeSug1) were synthesized in our laboratory in accordance with our previous work [6 (link),8 (link)]. The chemical structures of the bioselenocompounds used in this study are shown in Figure 1.

Takahashi K., Suzuki N, & Ogra Y. (2017). Bioavailability Comparison of Nine Bioselenocompounds In Vitro and In Vivo. International Journal of Molecular Sciences, 18(3), 506.

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Synthesis of Selenomethionine-containing RADA Peptide

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(Ac-RADARADARADARADA-NH2) and mRADA (Ac-RADARADARADARADG-NH2) were synthesized as previously reported [27] (link). For the synthesis of mRADA with selenomethionine (Ac-RADARADARADARADGSem-NH2), Fmoc-Sem-OH was prepared by the following procedure. To an aqueous solution (5 mL) of seleno-L-methionine (0.188 g, 0.959 mmol, Nacalai Tesque, Kyoto, Japan) and NaHCO3 (0.193 g, 2.30 mmol, Kishida Chemical, Tokyo, Japan) a 1,4-dioxane solution (10 mL, Kishida Chemical, Tokyo, Japan) of Fmoc-OSu (0.344 g, 1.02 mmol, Watanabe Chemical Industries, Hiroshima, Japan) was added dropwise over 90 min. After stirring for 24 h at 25°C, 2 M HCl aq. was added to acidify the reaction mixture to pH 3. The reaction mixture was extracted with EtOAc (10 mL, three times), and the collected organic phase was washed with saturated NH4Cl aq. (10 mL, once) and water (10 mL, twice). The organic phase was dried with Na2SO4. After filtration to remove insoluble substances, the organic phase was evaporated. The residue was separated on Sfär Silica HC D High Capacity Duo 20 μm using Isolera flash column chromatography of Biotage (Uppsala, Sweden) with a gradient elution between EtOAc and hexane (5/

Ohno Y., Nakajima C., Ajioka I., Muraoka T., Yaguchi A., Fujioka T., Akimoto S., Matsuo M., Lotfy A., Nakamura S., Herranz-Pérez V., García-Verdugo J.M., Matsukawa N., Kaneko N, & Sawamoto K. (2023). Amphiphilic peptide-tagged N-cadherin forms radial glial-like fibers that enhance neuronal migration in injured brain and promote sensorimotor recovery. Biomaterials, 294.

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