133083-36-0

Basic information

• Product Name: N'-(tert-Butoxycarbonyl)-N-(9-fluorenylmethyloxycarbonyl)-D-lysine pentafluorophenyl ester
• Synonyms: FMOC-N-EPSILON-BOC-D-LYSINE PENTAFLUOROPHENYL ESTER;FMOC-D-LYSINE(BOC)-OPFP;FMOC-D-LYS(BOC)-OPFP;N'-(tert-Butoxycarbonyl)-N-(9-fluorenylmethyloxycarbonyl)-D-lysine pentafluorophenyl ester;(R)-perfluorophenyl 1-(9H-fluoren-9-yl)-13,13-dimethyl-3,11-dioxo-2,12-dioxa-4,10-diazatetradecane-5-carboxylate;N-alpha-FMoc-N-epsilon-Boc-D-lysine pentafluorophenyl ester;N6-Boc-N2-Fmoc-D-Lysine pentafluorophenyl ester;(9H-Fluoren-9-yl)MethOxy]Carbonyl D-Lys(Boc)-OPfp
• CAS NO: 133083-36-0
• Molecular Formula: C₃₂H₃₁F₅N₂O₆
• Molecular Weight: 634.59
• Product Categories: Fmoc-Amino Acids and Derivatives;Fmoc-Amino acid series
• Mol File: 133083-36-0.mol

Chemical Properties

• Boiling Point: 726.742 °C at 760 mmHg
• Flash Point: 393.319 °C
• Appearance: /
• Density: 1.324
• Refractive Index: 1.543
• Storage Temp.: -15°C
• PKA: 10.27±0.46(Predicted)
• CAS DataBase Reference: N'-(tert-Butoxycarbonyl)-N-(9-fluorenylmethyloxycarbonyl)-D-lysine pentafluorophenyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: N'-(tert-Butoxycarbonyl)-N-(9-fluorenylmethyloxycarbonyl)-D-lysine pentafluorophenyl ester(133083-36-0)
• EPA Substance Registry System: N'-(tert-Butoxycarbonyl)-N-(9-fluorenylmethyloxycarbonyl)-D-lysine pentafluorophenyl ester(133083-36-0)

Safety Data

• Hazardous Substances Data: 133083-36-0(Hazardous Substances Data)

Usage

Uses

Used in Peptide Synthesis:
N'-(tert-Butoxycarbonyl)-N-(9-fluorenylmethyloxycarbonyl)-D-lysine pentafluorophenyl ester is used as a protected amino acid in peptide synthesis for the incorporation of D-lysine residues. The protection groups ensure that the lysine side chain does not participate in unwanted side reactions during the synthesis process, while the pentafluorophenyl ester group enhances the reactivity of the compound, allowing for efficient coupling with other peptide fragments.
Used in Research Applications:
In the field of research, N'-(tert-Butoxycarbonyl)-N-(9-fluorenylmethyloxycarbonyl)-D-lysine pentafluorophenyl ester is used as a key component in the synthesis of custom peptides for studying protein structures and functions. N'-(tert-Butoxycarbonyl)-N-(9-fluorenylmethyloxycarbonyl)-D-lysine pentafluorophenyl ester's ability to be selectively incorporated and later removed from peptides allows researchers to probe the effects of specific amino acid sequences on protein folding, stability, and interactions with other biomolecules.
Used in Pharmaceutical Development:
N'-(tert-Butoxycarbonyl)-N-(9-fluorenylmethyloxycarbonyl)-D-lysine pentafluorophenyl ester is employed in the pharmaceutical industry for the development of custom peptides with therapeutic potential. N'-(tert-Butoxycarbonyl)-N-(9-fluorenylmethyloxycarbonyl)-D-lysine pentafluorophenyl ester's versatility in peptide synthesis enables the creation of peptides with specific biological activities, such as enzyme inhibitors, receptor agonists or antagonists, or molecules with immunomodulatory properties. These custom peptides can be further optimized and tested for their efficacy and safety in treating various diseases and conditions.
Used in Drug Delivery Systems:
In drug delivery applications, N'-(tert-Butoxycarbonyl)-N-(9-fluorenylmethyloxycarbonyl)-D-lysine pentafluorophenyl ester can be used to synthesize peptides that serve as carriers or targeting moieties for drug molecules. N'-(tert-Butoxycarbonyl)-N-(9-fluorenylmethyloxycarbonyl)-D-lysine pentafluorophenyl ester's ability to be selectively incorporated and removed from peptides allows for the design of drug delivery systems with precise control over the release and targeting of therapeutic agents, potentially improving the efficacy and reducing the side effects of drug treatments.
Used in Bioconjugation:
N'-(tert-Butoxycarbonyl)-N-(9-fluorenylmethyloxycarbonyl)-D-lysine pentafluorophenyl ester is also used in the field of bioconjugation, where it can be employed to attach peptides to other biomolecules, such as proteins, nucleic acids, or nanoparticles. N'-(tert-Butoxycarbonyl)-N-(9-fluorenylmethyloxycarbonyl)-D-lysine pentafluorophenyl ester's reactivity and protection groups enable the formation of stable covalent bonds between peptides and other biomolecules, facilitating the development of conjugates with applications in diagnostics, therapeutics, or biosensing.

InChI:InChI=1/C32H31F5N2O6/c1-32(2,3)45-30(41)38-15-9-8-14-22(29(40)44-28-26(36)24(34)23(33)25(35)27(28)37)39-31(42)43-16-21-19-12-6-4-10-17(19)18-11-5-7-13-20(18)21/h4-7,10-13,21-22H,8-9,14-16H2,1-3H3,(H,38,41)(H,39,42)/t22-/m1/s1

Upstream product

• 771-61-9 2,3,4,5,6-pentafluorophenol 
• 92122-45-7 Fmoc-D-Lys(BOC)-OH 

Relevant articles and documents

Total Chemical Synthesis and Folding of All- l and All- d Variants of Oncogenic KRas(G12V)

The Ras proteins are essential GTPases involved in the regulation of cell proliferation and survival. Mutated oncogenic forms of Ras alter effector binding and innate GTPase activity, leading to deregulation of downstream signal transduction. Mutated forms of Ras are involved in approximately 30% of human cancers. Despite decades of effort to develop direct Ras inhibitors, Ras has long been considered "undruggable" due to its high affinity for GTP and its lack of hydrophobic binding pockets. Herein, we report a total chemical synthesis of all-l- and all-d-amino acid biotinylated variants of oncogenic mutant KRas(G12V). The protein is synthesized using Fmoc-based solid-phase peptide synthesis and assembled using combined native chemical ligation and isonitrile-mediated activation strategies. We demonstrate that both KRas(G12V) enantiomers can successfully fold and bind nucleotide substrates and binding partners with observable enantiodiscrimination. By demonstrating the functional competency of a mirror-image form of KRas bound to its corresponding enantiomeric nucleotide triphosphate, this study sets the stage for further biochemical studies with this material. In particular, this protein will enable mirror-image yeast surface display experiments to identify all-d peptide ligands for oncogenic KRas, providing a useful tool in the search for new therapeutics against this challenging disease target.

Solution phase synthesis of β-peptides using micro reactors

The synthesis of β-peptides has been successfully performed using a borosilicate glass micro reactor, in which a network of channels has been produced using a photolithographic and wet etching method. The reagents were mobilised by electroosmotic flow (EOF). The micro reactor was initially evaluated using a carbodiimide coupling reaction to form a dipeptide. The methodology has been extended such that the peptides may also be produced via the pentafluorophenyl ester derivatives of amino acids. It was found that performing the pentafluorophenyl ester reactions in the micro reactor resulted in an increase in the reaction efficiency over the traditional batch method. We postulate that the enhancement in rate of reaction is an electrochemical phenomenon, due to the reaction being performed in an electric field, which is unique to micro reactor systems. It has also been demonstrated that selective deprotection of the resultant dipeptides can be achieved. This approach has been used in the synthesis of a tripeptide.