101555-63-9

Basic information

• Product Name: FMOC-D-PIPECOLIC ACID
• Synonyms: (R)-PIPERIDINE-1,2-DICARBOXYLIC ACID 1-(9H-FLUOREN-9-YLMETHYL) ESTER;(R)-N-FLUORENYLMETHOXYCARBONYL-2-PIPERIDINECARBOXYLIC ACID;(R)-N-FMOC-PIPERIDINE-2-CARBOXYLIC ACID;(R)-N-(9-FLUORENYLMETHYLOXYCARBONYL)-PIPERIDINE-2-CARBOXYLIC ACID;RARECHEM AR PA 0006;N-ALPHA-(9-FLUORENYLMETHOXYCARBONYL)-D-PIPECOLIC ACID;N-ALPHA-(9-FLUORENYLMETHOXYCARBONYL)-D-HOMOPROLINE;N-ALPHA-FMOC-D-PIPECOLIC ACID
• CAS NO: 101555-63-9
• Molecular Formula: C₂₁H₂₁NO₄
• Molecular Weight: 351.4
• Product Categories: Unusual amino acids;chiral;Pyridine;Amino Acids
• Mol File: 101555-63-9.mol

Chemical Properties

• Melting Point: 149-153°C
• Boiling Point: 561.6 °C at 760 mmHg
• Flash Point: 293.5 °C
• Appearance: White to pale brown/Solid
• Density: 1.293 g/cm³
• Vapor Pressure: 1.89E-13mmHg at 25°C
• Refractive Index: 1.62
• Storage Temp.: 2-8°C
• Solubility: soluble in Methanol
• PKA: 3.97±0.20(Predicted)
• BRN: 5485101
• CAS DataBase Reference: FMOC-D-PIPECOLIC ACID(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-D-PIPECOLIC ACID(101555-63-9)
• EPA Substance Registry System: FMOC-D-PIPECOLIC ACID(101555-63-9)

Safety Data

• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 26-36-37/39
• RIDADR: 3077
• WGK Germany: 3
• HazardClass: IRRITANT
• Hazardous Substances Data: 101555-63-9(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
FMOC-D-PIPECOLIC ACID is used as a building block for the preparation of cyclic tetrapeptide derivatives. These derivatives have potential applications as histone deacetylase inhibitors and antitumor agents, making them valuable in the development of new drugs for cancer treatment.
Used in Chemical Research:
As a building block, FMOC-D-PIPECOLIC ACID is also used in chemical research for the synthesis of various compounds with potential applications in different industries. Its unique chemical properties make it a versatile component in the development of new materials and products.

InChI:InChI=1/C21H21NO4/c23-20(24)19-11-5-6-12-22(19)21(25)26-13-18-16-9-3-1-7-14(16)15-8-2-4-10-17(15)18/h1-4,7-10,18-19H,5-6,11-13H2,(H,23,24)/t19-/m1/s1

Upstream product

• 28920-43-6 (fluorenylmethoxy)carbonyl chloride 
• 15912-30-8 (2S)-2-piperidinecarboxylic acid L-tartrate 
• 88744-04-1 (9-fluorenyl)methyl pentafluorophenyl carbonate 
• 3105-95-1 pipecolinic acid 
• 82911-69-1 N-(9H-fluoren-2-ylmethoxycarbonyloxy)succinimide 
• 4043-87-2 pipecolic Acid 
• 15912-30-8 (R)-(+)-2-piperidinecarboxylic acid (+)-tartrate 
• 1723-00-8 (R)-(+)-pipecolic acid 
• 102774-86-7 9-fluorenylmethyl N-succinimidyl carbonate 

Downstream Products

• 86060-91-5 Fmoc-Pip-Pfp 
• 195202-02-9 (S)-1-(9H-fluoren-9-yl)methyl 2-((R)-1-(3-(2-tert-butoxy-2-oxo-ethoxy) phenyl)-3-(3,4-dimethoxyphenyl)propyl) piperidine-1,2-dicarboxylate 
• 507267-90-5 Z-Aib-Aib-Pip-Aib-Gly-OH 
• 195202-03-0 (S)-((R)-1-(3-(2-tert-butoxy-2-oxoethoxy)phenyl)-3-(3,4-dimethoxyphenyl)-propyl) piperidine-2-carboxylate 

Relevant articles and documents

Brain-targeted chemical delivery of [Leu2, Pip3]-TRH: Synthesis and biological evaluation

A chemical targeting system for [Leu2, Pip3]-TRH (Gln,Leu,Pip) was synthesized in order to allow its specific delivery to the central nervous system (CNS). Sequential metabolism of the obtained 'packaged' chemical delivery system, (CDS), DHT-Pro-Pro-Gln-Leu-Pip-OCh, should yield a 'locked- in' precursor following the oxidative conversion of the dihydrotrigonellyl (DHT) to the trigonellyl (T+) moiety, followed by removal of the cholesteryl function and cleavage of the T+-Pro-Pro by prolyl endopeptidase. The antagonism of barbiturate-induced sleeping time was used to assess the activity of the CDS. The sleeping time after administration of vehicle and [Leu2]-TRH was 100.5 ± 6.3 min, and 78.2 ± 4.7 min, respectively. The [Leu2, Pip3]-TRH-CDS showed a significant decrease in sleeping time (58.2 ± 3.4 min) compared to the vehicle or [Leu2]-TRH. These results indicate successful brain delivery of the precursor construct, and an effective release of the active GlnLeuPip in the brain. (C) 2000 Elsevier Science Ltd.

Synthesis of Shld Derivatives, Their Binding to the Destabilizing Domain, and Influence on Protein Accumulation in Transgenic Plants

A series of 35 analogues of Shld with modifications in the A-residue and the C-residues were prepared and investigated for binding to FKBP and GFP accumulation in transgenic plants. The modifications investigated explored variations that were supposedly i

2-ARYLSULFONAMIDO-N-ARYLACETAMIDE DERIVATIZED STAT3 INHIBITORS

The present disclosure provides pharmaceutical compositions comprising 2-arylsulfonamido-N-arylacetamide derivatized Stat3 inhibitors and certain pharmaceutically acceptable salts thereof, and methods of their use.

Heterocyclic core analogs of a direct thrombin inhibitor

Thrombin is a serine protease that plays a key role in blood clotting. Pyrrolidine 1 is a potent thrombin inhibitor discovered at Merck several years ago. Seven analogs (2-8) of 1 in which the pyrrolidine core was replaced with various heterocycles were p

THROMBIN INHIBITORS

Compounds of the invention are useful in inhibiting thrombin and associated thrombotic occlusions having the following structure: (I) or a pharmaceutically acceptable salt thereof, wherein Q is CH2, NR4, O, S, S(O) or S(O2

PIPECOLATE-DIKETOAMIDES FOR TREATMENT OF PSYCHIATRIC DISORDERS

The present invention relates to compounds having a pipecolate diketoamide scaffold, pharmaceutically acceptable salts of these compounds and pharmaceutical compositions containing at least one of these compounds together with pharmaceutically acceptable carrier, excipient and/or diluents. Said pipecolate diketoamide compounds can be used for prophylaxis and/or treatment of psychiatric disorders and neurodegenerative diseases, disorders and conditions.

Pipecolate-diketoamides for treatment of psychiatric disorders

The present invention relates to compounds having a pipecolate diketoamide scaffold, pharmaceutically acceptable salts of these compounds and pharmaceutical compositions containing at least one of these compounds together with pharmaceutically acceptable

Evaluation of synthetic FK506 analogues as ligands for the FK506-binding proteins 51 and 52

The FK506-binding proteins (FKBP) 51 and 52 are cochaperones that modulate the signal transduction of steroid hormone receptors. Both proteins have been implicated in prostate cancer. Furthermore, single nucleotide polymorphisms in the gene encoding FKBP51 have been associated with a variety of psychiatric disorders. Rapamycin and FK506 are two macrocyclic natural products that bind to these proteins indiscriminately but with nanomolar affinity. We here report the cocrystal structure of FKBP51 with a simplified α-ketoamide analogue derived from FK506 and the first structure-activity relationship analysis for FKBP51 and FKBP52 based on this compound. In particular, the tert-pentyl group of this ligand was systematically replaced by a cyclohexyl ring system, which more closely resembles the pyranose ring in the high-affinity ligands rapamycin and FK506. The interaction with FKBPs was found to be surprisingly tolerant to the stereochemistry of the attached cyclohexyl substituents. The molecular basis for this tolerance was elucidated by X-ray cocrystallography.

Total synthesis of the antifungal depsipeptide petriellin A

We report the solid-phase total synthesis of the antifungal highly modified cyclic depsipeptide petriellin A. The synthesis confirms earlier reports on the absolute configuration of the natural product. The solid-phase approach resulted in a protected lin

Biosynthesis of pipecolic acid by RapL, a lysine cyclodeaminase encoded in the rapamycin gene cluster

Rapamycin, FK506, and FK520 are immunosuppressant macrolactone natural products comprised of predominantly polyketide-based core structures. A single nonproteinogenic pipecolic acid residue is installed into the scaffold by a nonribosomal peptide synthetase that also performs the subsequent macrocyclization step at the carbonyl group of this amino acid. It has been assumed that pipecolic acid is generated from lysine by the cyclodeaminases RapL/FkbL. Herein we report the heterologous overexpression and purification of RapL and validate its ability to convert L-lysine to L-pipecolic acid by a cyclodeamination reaction that involves redox catalysis. RapL also accepts L-ornithine as a substrate, albeit with a significantly reduced catalytic efficiency. Turnover is presumed to encompass a reversible oxidation at the α-amine, internal cyclization, and subsequent re-reduction of the cyclic Δ1-piperideine-2-carboxylate intermediate. As isolated, RapL has about 0.17 equiv of tightly bound NAD+, suggesting that the enzyme is incompletely loaded when overproduced in E. coli. In the presence of exogenous NAD+, the initial rate is elevated 8-fold with a K m of 2.3 μM for the cofactor, consistent with some release and rebinding of NAD+ during catalytic cycles. Through the use of isotopically labeled substrates, we have confirmed mechanistic details of the cyclodeaminase reaction, including loss of the α-amine and retention of the hydrogen atom at the α-carbon. In addition to the characterization of a critical enzyme in the biosynthesis of a medically important class of natural products, this work represents the first in vitro characterization of a lysine cyclodeaminase, a member of a unique group of enzymes which utilize the nicotinamide cofactor in a catalytic manner.