Name: Azido palmitic acid
Brand: BOC Sciences
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Synonyms

15-Azidopentadecanoic acid

IUPAC Name

15-azidopentadecanoic acid

Canonical SMILES

C(CCCCCCCN=[N+]=[N-])CCCCCCC(=O)O

InChI

InChI=1S/C15H29N3O2/c16-18-17-14-12-10-8-6-4-2-1-3-5-7-9-11-13-15(19)20/h1-14H2,(H,19,20)

InChIKey

PYGQAGHMXCCROO-UHFFFAOYSA-N

Appearance

White crystalline

Storage

Store at -20 °C, desiccate and shipped at ambient temperature

Azido palmitic acid is a versatile chemical compound with numerous applications in biological research and bioconjugation. Here are some key applications of azido palmitic acid:

Metabolic Labeling: Azido palmitic acid is used in metabolic labeling to incorporate azide groups into biomolecules such as proteins and lipids. These azide-modified molecules can then be tagged with fluorescent dyes or other probes using click chemistry, allowing researchers to track their dynamics in living cells. This application is invaluable for studying protein localization, trafficking, and interactions within cellular environments.

Protein Lipidation Studies: Azido palmitic acid serves as a probe for investigating protein lipidation, specifically S-palmitoylation. By incorporating this azido fatty acid into cellular proteins, researchers can identify and characterize palmitoylated proteins through subsequent bioorthogonal ligation reactions. This helps in understanding the functional roles of lipid modifications in signal transduction, membrane association, and protein stability.

Bioorthogonal Chemistry: Due to its azide functional group, azido palmitic acid is an essential tool in bioorthogonal chemistry, facilitating the selective modification of biomolecules in complex biological systems. It allows for specific conjugation reactions without interfering with native biochemical processes. This selective reactivity is used in a wide range of applications, including the development of diagnostic assays and targeted drug delivery systems.

Cell Membrane Studies: Azido palmitic acid can be utilized to label and study cell membrane components, providing insights into lipid-protein interactions and membrane dynamics. By incorporating azido-functionalized lipids into cellular membranes, researchers can visualize and analyze membrane organization and properties using fluorescence microscopy. This approach is crucial for exploring membrane-associated processes such as endocytosis, signal transduction, and cell-cell communication.

1. Photoreactive fatty acid analogues that bind to the rat liver fatty-acid binding protein: 11-(5'-azido-salicylamido)-undecanoic acid derivatives

F Atlasovich, J A Santomé, H N Fernández Mol Cell Biochem. 1993 Mar 10;120(1):15-23. doi: 10.1007/BF00925980.

Photoreactive probes for the hydrophobic pocket of the liver fatty acid-binding protein, 11-(5'-azido-salicylamido)-undecanoic acid (5' ASU) and its acetyl ester (Ac5' ASU), were synthesized and their interaction with the protein was assessed. Fatty acid-binding proteins are closely related proteins which are abundantly expressed in tissues with active lipid metabolism. A simple model that assumes that the protein possesses a single kind of sites fitted the binding of radioiodinated 5' ASU to L-FABP satisfactorily. The apparent dissociation constant, 1.34 x 10(-7) M, evidenced a slightly higher affinity than that reported for C16-C20 fatty acids. Consistent with the binding curve, 5' ASU effectively competed with palmitic acid for the hydrophobic sites and the effect was nearly complete for concentrations of 1 microM; oleic acid, in turn, displaced the radiolabelled probe. Irradiation at 366 nm of 125I-5' ASU bound to L-FABP caused the covalent cross-linking of the reagent. The amount of radioactivity covalently bound reached a maximum after 2 min thus agreeing with the photo-activation kinetics of the unlabelled compound that evidenced a t1/2 of 31.1 sec. The yield with which probes bound to L-FABP became covalently linked to the protein, appraised after SDS-PAGE of irradiated samples, was estimated as 23 and 26 per cent for 5' ASU and Ac5' ASU respectively. In turn, irradiation of L-FABP incubated with 5' ASU or Ac5' ASU resulted in the irreversible loss of about one fourth its ability to bind palmitic acid.(ABSTRACT TRUNCATED AT 250 WORDS)

2. Synthesis and characterization of bichromophoric 1-deoxyceramides as FRET probes

Eduardo Izquierdo, Mireia Casasampere, Gemma Fabriàs, José Luís Abad, Josefina Casas, Antonio Delgado Org Biomol Chem. 2021 Mar 21;19(11):2456-2467. doi: 10.1039/d1ob00113b. Epub 2021 Mar 2.

The suitability as FRET probes of two bichromophoric 1-deoxydihydroceramides containing a labelled spisulosine derivative as a sphingoid base and two differently ω-labelled fluorescent palmitic acids has been evaluated. The ceramide synthase (CerS) catalyzed metabolic incorporation of ω-azido palmitic acid into the above labeled spisulosine to render the corresponding ω-azido 1-deoxyceramide has been studied in several cell lines. In addition, the strain-promoted click reaction between this ω-azido 1-deoxyceramide and suitable fluorophores has been optimized to render the target bichromophoric 1-deoxydihydroceramides. These results pave the way for the development of FRET-based assays as a new tool to study sphingolipid metabolism.

3. Photoactivated azido fatty acid irreversibly inhibits anion and proton transport through the mitochondrial uncoupling protein

P Jezek, J Hanus, C Semrad, K D Garlid J Biol Chem. 1996 Mar 15;271(11):6199-205. doi: 10.1074/jbc.271.11.6199.

The protonophoretic function of uncoupling protein (UCP) is activated by fatty acids. According to the "docking site" hypothesis (Jezek, P., and Garlid, K. D., J. Biol. Chem. 265, 19303-19311, 1990), the fatty acid binding site is identical with the anion channel of UCP. Skulachev (Skulachev, V. P. (1991) FEBS Lett. 294, 158-162) extended this hypothesis by suggesting that fatty acid anions are transported by UCP and that H+ are delivered by back-diffusion of the protonated fatty acid through the lipid bilayer. In this model, UCP does not transport H+ at all but rather enables fatty acids to act as cycling protonophores. New evidence supports this mechanism (Garlid, K. D., Orosz, D. E., Modriansky, M., Vassanelli, S., and Jezek, P. (1996) J. Biol. Chem. 271, 2615-2620). To help elucidate these hypotheses, we synthesized a photoreactive analog of dodecanoic acid, 12-(4-azido-2-nitrophenylamino)dodecanoic acid (AzDA), and studied its effect on transport in mitochondria and proteoliposomes. AzDA behaved in every respect like a typical fatty acid. In micromolar doses, AzDA activated H+ translocation and inhibited Cl- and hexanesulfonate uniport through UCP. After UV light exposure, however, activation of H+ transport was inhibited, whereas inhibition of anion transport was preserved. These effects were irreversible. Photolabeling of mitochondria with [3H]AzDA resulted in a prominent 32 kDa band of UCP, and few other proteins were labeled. The results indicate that AzDA can be ligated to the protein at or near the docking site, causing irreversible inhibition of both H+ and anion transport. The finding that fatty acid-induced H+ transport disappears along with anion transport supports the fatty acid-protonophore mechanism of H+ transport by UCP.