Palmitic Acid Alkyne

Protein S-palmitoylation is the post-translational acylation of proteins and serves to regulate localization, stability, and interaction with associates and substrates.[1] Palmitic acid alkyne is a form of palmitic acid with an ω-terminal alkyne. The terminal alkyne group can be used in linking reactions, known as click chemistry; this chemistry is characterized by high dependability and specificity of the azide-alkyne bioconjugation reactions. [2] [3]The use of palmitic acid alkyne and related lipids in isolating palmitoylated proteins has been described. [4] [5] [6]

Reference:
[1]. Aicart-Ramos, C., Valero, R.A., and Rodriguez-Crespo, I. Protein palmitoylation and subcellular trafficking. Biochimica et Biophysica Acta 1808, 2981-2994 (2011).
[2]. Kolb, H.C., and Sharpless, K.B. The growing impact of click chemistry on drug discovery. Drug Discov. Today 8(24), 1128-1137 (2003).
[3]. Lutz, J.F., and Zarafshani, Z. Efficient construction of therapeutics, bioconjugates, biomaterials and bioactive surfaces using azide-alkyne "click" chemistry. Adv. Drug Deliv. Rev. 60(9), 958-970 (2008).
[4]. Martin, B.R., and Cravatt, B.F. Large-scale profiling of protein palmitoylation in mammalian cells. Nat. Methods 6(2), 135-138 (2009).
[5]. Yap, M.C., Kostiuk, M.A., Martin, D.D.O., et al. Rapid and selective detection of fatty acylated proteins using ω-alkynyl-fatty acids and click chemistry. Journal of Lipid Research 51, 1566-1580 (2010).
[6]. Jiang, H., Khan, S., Wang, Y., et al. SIRT6 regulates TNF-α secretion through hydrolysis of long-chain fatty acyl lysine. Nature 496, 110-113 (2013).