O-(2-Aminoethyl)-O’-(2-azidoethyl)tetraethylene Glycol

• CAT Number: R054686
• CAS Number: 516493-93-9
• Molecular Formula: C12H26N4O5
• Molecular Weight: 306.363
• Purity: ≥95%
• Synonyms: 17-Azido-3,6,9,12,15-pentaoxaheptadecan-1-amine;Azido-PEG5-Amine； N3-PEG5-CH2CH2NH2。
• Target: PROTAC Linkers
• Storage: Store at -20C
• IUPAC Name: 2-[2-[2-[2-[2-(2-azidoethoxy)ethoxy]ethoxy]ethoxy]ethoxy]ethanamine
• InChI: InChI=1S/C12H26N4O5/c13-1-3-17-5-7-19-9-11-21-12-10-20-8-6-18-4-2-15-16-14/h1-13H2
• InChIKey: SVPBRIZYFJFLOL-UHFFFAOYSA-N
• SMILES: C(COCCOCCOCCOCCOCCN=[N+]=[N-])N

Amino-PEG5-azide(CAS: 516493-93-9） is developed as a bifunctional PEG reagent with great solubility in aqueous media. The amino group is reactive with carboxylic acids, activated NHS esters. The azide group can react with alkyne, BCN, DBCO via Click Chemistry to yield a stable triazole linkage.

Reference

[1]. Yuan, S., Chu, H., Chan, J.F.W., Ye, Z.W., Wen, L., Yan, B., Lai, P.M., Tee, K.M., Huang, J., Chen, D. and Li, C., 2019.
SREBP-dependent lipidomic reprogramming as a broad-spectrum antiviral target.
Abstract: Viruses are obligate intracellular microbes that exploit the host metabolic machineries to meet their biosynthetic demands, making these host pathways potential therapeutic targets. Here, by exploring a lipid library, we show that AM580, a retinoid derivative and RAR-α agonist, is highly potent in interrupting the life cycle of diverse viruses including Middle East respiratory syndrome coronavirus and influenza A virus. Using click chemistry, the overexpressed sterol regulatory element binding protein (SREBP) is shown to interact with AM580, which accounts for its broad-spectrum antiviral activity. Mechanistic studies pinpoint multiple SREBP proteolytic processes and SREBP-regulated lipid biosynthesis pathways, including the downstream viral protein palmitoylation and double-membrane vesicles formation, that are indispensable for virus replication. Collectively, our study identifies a basic lipogenic transactivation event with broad relevance to human viral infections and represents SREBP as a potential target for the development of broad-spectrum antiviral strategies.
Nature communications, 10(1), pp.1-15.