L-Homopropargyl Glycine is a synthetic bioorthogonal non-canonical amino acid probe used for the study of protein synthesis. L-Homopropargyl Glycine is widely used in biochemical research to monitor protein synthesis within cells[1]. When cells take up L-Homopropargyl Glycine, L-Homopropargyl Glycine is incorporated into the proteins being synthesized, replacing methionine. Through the Cu(I)-catalyzed azide-alkyne cycloaddition (CuAAC) reaction, biotin or other fluorescently labeled azides can be conjugated to proteins labeled with L-Homopropargyl Glycine, thereby enabling the capture, enrichment, and detection of newly synthesized proteins [2].
References:
[1] Tivendale ND, Fenske R, Duncan O, et al. In vivo homopropargylglycine incorporation enables sampling, isolation and characterization of nascent proteins from Arabidopsis thaliana. Plant J. 2021 Aug;107(4):1260-1276.
[2] Shen Y, Liu W, Zuo J, et al. Protocol for visualizing newly synthesized proteins in primary mouse hepatocytes. STAR Protoc. 2021 Jun 17;2(3):100616.
L-Homopropargyl Glycine是一种用于研究蛋白质合成的合成型生物正交非天然氨基酸探针。L-Homopropargyl Glycine广泛应用于生物化学研究中，用于监测细胞内蛋白质的合成情况[1]。当细胞摄取L-Homopropargyl Glycine后，L-Homopropargyl Glycine会被整合到正在合成的蛋白质中，取代甲硫氨酸的位置。通过Cu(I)催化的叠氮-炔烃环加成反应（CuAAC），可以将带有生物素或其他荧光标记的叠氮化物与HPG标记的蛋白质进行共轭反应，从而实现对新合成蛋白质的捕获、富集和检测[2]。