14464-31-4

Usage

Uses

Used in Pharmaceutical Industry:
N-Succinimidyl palmitate is used as a synthetic intermediate for the preparation of various biologically active molecules, such as N-acylamino acids, aminoacyl-tRNA, coenzyme A, thioglycolic acid, and ceramides. These molecules play crucial roles in various biological processes and have potential applications in the development of new drugs and therapies.
Used in Biochemical Research:
N-Succinimidyl palmitate is used as a labeling agent for primary amines in proteins, amine-modified oligonucleotides, and other amine-containing molecules. This application is essential in biochemical research, as it allows for the tracking and identification of specific molecules within complex biological systems.
Used in Diagnostics:
The ability of N-succinimidyl palmitate to label primary amines can also be utilized in the development of diagnostic tools. By attaching the compound to specific target molecules, it can help in the detection and monitoring of various diseases and conditions.
Used in Drug Delivery Systems:
N-Succinimidyl palmitate can be employed in the design and development of drug delivery systems, where it can be used to modify the surface of drug carriers or to attach drugs to targeting molecules, enhancing the specificity and efficacy of the treatment.

InChI:InChI=1/C20H35NO4/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-20(24)25-21-18(22)16-17-19(21)23/h2-17H2,1H3

Upstream product

• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 57-10-3 1-hexadecylcarboxylic acid 
• 123-56-8 Succinimide 
• 112-67-4 n-hexadecanoyl chloride 
• 5672-89-9 N-trifluoroacetoxy succinimide 

Downstream Products

• 56255-31-3 N-n-hexadecanoyl (L)-alanine 
• 59012-43-0 (S)-α-Palmitoyl-N_ε-lysine 
• 1782-17-8 N-hexadecanoyl-L-aspartic acid 
• 2441-41-0 N-palmitoyl glycine 
• 52558-68-6 N-hexadecanoyl-β-alanine 
• 21394-64-9 N-palmitoyl-L-serine 
• 17627-10-0 dipalmitoyl cystine 
• 95399-77-2 (S)-3-(4-hydroxyphenyl)-2-palmitamidopropanoic acid 
• 59441-32-6 (S)-1-palmitoylpyrrolidine-2-carboxylic acid 
• 24583-16-2 6-O-hexadecanoyl-methyl-α-D-glucopyranoside 
• 24613-33-0 methyl 2-O-palmitoyl-α-D-glucopyranoside 
• 66891-06-3 methyl 3-O-palmitoyl-α-D-glucopyranoside 
• 188048-67-1 Palm-Ser(Bzl)-Asp(OBzl)-Ala-Arg(NO₂)-OMe 
• 58725-44-3 GABA-palmitamide 

Relevant academic research and scientific papers

Functionalization of poly(amidoamine) dendrimers with hydrophobic chains for improved gene delivery in mesenchymal stem cells

A new family of gene delivery vectors is synthesized consisting of a medium-size generation PAMAM dendrimer (generation 5, with amine termini) core randomly linked at the periphery to hydrophobic chains that vary in length (12 to 16 carbon alkyl chains) and number (from 4.2 to 9.7 in average). The idea subjacent to the present work is to join the advantages of the cationic nature of the dendrimer with the capacity of lipids to interact with biological membranes. Unlike other amphiphilic systems designed for the same purpose, where the hydrophobic and hydrophilic moieties coexist in opposite sides, the present vectors have a hydrophilic interior and a hydrophobic corona. The vectors are characterized in respect to their ability to neutralize, bind and compact plasmid DNA (pDNA). The complexes formed between the vectors and pDNA are analyzed concerning their size, ζ-potential, resistance to serum nucleases, capacity of being internalized by cells and transfection efficiency. These new vectors show a remarkable capacity for mediating the internalization of pDNA with minimum cytotoxicity, being this effect positively correlated with the -CH2- content present in the hydrophobic corona. Gene expression in MSCs, a cell type with relevancy in the regenerative medicine clinical context, is also enhanced using the new vectors but, in this case, the higher efficiency is shown by the vectors containing the smallest hydrophobic chains.

Luliberin analogues exhibiting a cytotoxic effect on tumor cells in vitro

Luliberin analogues modified at the N-terminus were synthesized to search for drugs exerting a cytotoxic effect on cells of hormone-dependent tumors. A synthetic scheme effective in the preparation of analogues containing fatty acid residues was proposed. The cytotoxic effect of the peptides was studied on a number of cell lines of human tumors in vitro. The dependence of the antitumor effect on the length of peptide chain, amino acid sequence, and structure of the N-terminal group was demonstrated. Modification with palmitic acid was found to result in highly active compounds in the case of analogues containing more than ten aa, whereas modifications with lauric, caproic, or trimethylacetic acid led to compounds with significantly lower activities. Analogues of luliberin containing a palmitic acid residue and effectively inhibiting the growth of tumor cells in vitro were synthesized. Pleiades Publishing, Inc., 2006.

Chemical modification of recombinant hirudin with palmitic acid in mixed aqueous-organic solutions

In this study, chemical modification of recombinant hirudin variant-2 (HV2) with palmitic acid (PAL) was proposed as an alternative approach to circumvent the limitations of PEGylation. To facilitate a sufficient contact of the hydrophilic HV2 to the hydrophobic PAL, thereby improving the reaction specificity to achieve the desired mono-PAL-HV2 with high retained bioactivity, the reaction was developed in mixed aqueous-organic solutions. Compared with HV2 conjugation with PAL-benzotriazole (PAL-BTA) in mixed aqueous-NMP solution, the conjugation of HV2 with PAL-N-hydroxysuccinimide (PAL-NHS) in mixed aqueous-DMSO solution could improve the site-specific conjugation of one PAL molecule to a particular lysine residue. Furthermore, the reaction mixture of the latter was further purified by preparative liquid chromatography. Three mono-PAL-HV2 isomers were obtained and retained 36%, 4% and 89% of the in vitro anticoagulant activity of unmodified HV2, respectively. One of the mono-PAL-HV2 isomers, namely, mono-PAL-HV2-3, was isolated with the highest selectivity and exhibited the highest in vitro anticoagulant bioactivity. Modification site analysis of mono-PAL-HV2-3 revealed that a single PAL molecule was conjugated at Lys27 of HV2. This study presented a successful PAL modification in which site-specific reaction was improved to achieve the desired mono-PAL-HV2 with highly retained bioactivity in mixed aqueous-organic solutions.

Chemoselective acylation of fully deprotected hydrazino acetyl peptides. Application to the synthesis of lipopeptides

Fully deprotected N-terminal α-hydrazino acetyl peptides were synthesized and chemoselectively acylated on the hydrazine moiety with various fatty acid succinimidyl esters or N-(cholesterylcarbonyloxy) succinimide to give lipopeptides of high purity. The buffer and pH were adjusted in order to minimize the oxidation of the hydrazine moiety and to achieve the best conversion and selectivity. The acylation was performed in a citrate - Phosphate buffer/2-methylpropan-2-ol mixture of pH 5.1. The pKa of the α-hydrazino acetyl group on our model peptide was found to be 6.45, i.e., about 2 units lower than the pKa of a glycyl residue. The reaction was subsequently applied to the synthesis of a 38AA peptide derivatized by a palmitoyl group.

Systematic exploration of lipophilic tags that allow efficient anchoring of aptamers to live cell surfaces

We carried out a systematic exploration of lipophilic tag molecules that allow efficient anchoring of aptamers to live cell surfaces. Among the lipids tested, the C16 dialkyl (dipalmitoylphosphatidylethanolamine) tag showed a good performance: a high anchoring yield and long retention on live cells. The 3'-C16 dialkyl tag-labeled fluorescent aptamer sensor, targeting thrombin, was prepared. The aptamer sensor was anchored successfully to live cells, allowing fluorescence detection of thrombin on the cell surface.

Innovative chemical synthesis and conformational hints on the lipopeptide liraglutide

Liraglutide is a new generation lipopeptide drug used for the treatment of type II diabetes. In this work, we describe new approaches for its preparation fully by chemical methods. The key step of these strategies is the synthesis in solution of the Lys/γ-Glu building block, Fmoc-Lys-(Pal-γ-Glu-OtBu)-OH, in which Lys and Glu residues are linked through their side chains and γ-Glu is Nα-palmitoylated. This dipeptide derivative is then inserted into the peptide sequence on solid phase. As liraglutide is obtained with great purity and high yield, our approach can be particularly attractive for an industrial production. We also report here the results of a circular dichroism conformational analysis in a membrane mimetic environment that offers new insights into the mechanism of action of liraglutide. Copyright

Palmitoyl derivatives of interferon α: Potential for cutaneous delivery

Palmitoyl derivatives of interferon α2b (p-IFNα) were prepared by covalent attachment of the fatty acid to lysine residues in the protein through a reaction with N-hydroxysuccinimide palmitate ester. The p-IFNα was characterized by capillary electrophoresis (CE), mass spectrometry (MS), SDS- PAGE, and antiviral assay. Flow-through diffusion cells and human breast skins were used to measure cutaneous and percutaneous absorption. Formation of p-IFNα derivatives was demonstrated by CE to be dependent on reaction time and reagent: protein ratio. Electrospray MS of the crude p-IFNα mixture indicated three populations of IFNα derivatives with 10, 11, and 12 palmitoyl substitutions. The addition of palmitoyl residues to IFNα under the conditions described reduced the antiviral specific activity by 50%. However, the cutaneous absorption of p-IFNα was about 5-6 times greater than the parent protein. The amount of p-IFNα and IFN α in whole skin after 24 h of treatment was 2.106 ± 1.216 μg/cm2 and 0.407 ± 0.108μg/cm2, respectively. Approximately two times higher flux was detected for p-IFNα compared to the nonfatty acylated IFNα. The total amount of drug diffused in 24 h was also approximately two times higher for the p-IFNα. The results indicate a potential for using fatty acylated derivatives of IFN α for dermal and transdermal delivery.

Blended polar/nonpolar peptide conjugate interferes with human insulin amyloid-mediated cytotoxicity

Insulin, a peptide hormone and a key regulator of blood glucose level, is routinely administered to type-I diabetic patients to achieve the required glycemic control. Insulin aggregation and ensuing amyloidosis has been observed at repeated insulin injection sites and in injectable formulations. The latter occurs due to insulin agglomeration during shipping and storage. Such insulin amyloid leads to enhanced immunogenicity and allow potential attachment to cell membranes leading to cell permeability and apoptosis. Small molecule inhibitors provide useful interruption of this process and inhibit protein misfolding as well as amyloid formation. In this context, we report the propensity of a palmitoylated peptide conjugate to inhibit insulin aggregation and amyloid-mediated cytotoxicity, via designed interference with polypeptide interfacial interactions.

Synthesis and Antitumor Activity of Conjugates Based on the Phe-D-Trp-Lys-Thr Peptide Fragment of Somatostatin

Abstract: New somatostatin analogs containing the fragments of adamantane, coumarin, tetrahydrocarbazole, and palmitic acid of the general formula R-Phe-D-Trp-Lys(Boc)-Thr-OMe have been synthesized. The structure of the conjugates combines a peptide fragm

COMPOUNDS AND METHODS FOR THE TREATMENT OF DUCHENNE MUSCULAR DYSTROPHY

Disclosed herein are compounds including a single-stranded oligonucleotide (A) having a nucleobase sequence complementary to a portion of the dystrophin pre-mRNA, their preparation, and uses thereof for the treatment of Duchenne muscular dystrophy.