69558-55-0

Basic information

• Product Name: Thymopentin
• Synonyms: 32-36-Thymopoietin;L-Arg-L-Lys-L-Asp-L-Val-L-Tyr-OH;Thymopoietin II-(32-36);ThyMopentin for Injection;ARG-LYS-ASP-VAL-TYR;(ASP34)-THYMOPOIETIN III (32-36) (BOVINE);H-ARG-LYS-ASP-VAL-TYR-OH;RKDVY
• CAS NO: 69558-55-0
• Molecular Formula: C₃₀H₄₉N₉O₉
• Molecular Weight: 268.93
• EINECS: 2017-001-1
• Product Categories: IMMUNOX;Inhibitors;Amino Acid Derivatives;Peptide
• Mol File: 69558-55-0.mol

Chemical Properties

• Appearance: White/Powder
• Density: 1.44 g/cm³
• Refractive Index: 1.635
• Storage Temp.: −20°C
• PKA: 3.07±0.10(Predicted)
• CAS DataBase Reference: Thymopentin(CAS DataBase Reference)
• NIST Chemistry Reference: Thymopentin(69558-55-0)
• EPA Substance Registry System: Thymopentin(69558-55-0)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 69558-55-0(Hazardous Substances Data)

Usage

Originator

Janssen (Belgium)

Uses

Different sources of media describe the Uses of 69558-55-0 differently. You can refer to the following data:
1. Thymopentin Acetate (TP-5) is a synthetic immunomodulating pentapeptide.
2. immunoregulator

Brand name

SINTOMODULINA; TIMUNOX

Clinical Use

Thymopentin is a synthetic, immunomodulating pentapeptide, representing the active fragment of the thymus hormone, thymopoietin. Thymopentin induces phenotypic differentiation and maturation of T-cells. It appears of value in the treatment of primary immune deficiency, rheumatoid arthritis, atopic dermatitis, sarcoidosis and a variety of other diseases with manifestations of disturbed immune balance.

References

Zhang, Yan, et al. "Novel thymopentin release systems prepared from bioresorbable PLA–PEG–PLA hydrogels." International journal of pharmaceutics 386.1 (2010): 15-22. Gonser, S., E. Weber, and G. Folkers. "Peptides and polypeptides as modulators of the immune response: thymopentin—an example with unknown mode of action." Pharmaceutica Acta Helvetiae 73.6 (1999): 265-273. Wang, Ying, et al. "Synthetic modifications of the immunomodulating peptide thymopentin to confer anti-mycobacterial activity." Biomaterials 35.9 (2014): 3102-3109.

InChI:InChI=1/C30H49N9O9/c1-16(2)24(28(46)38-22(29(47)48)14-17-8-10-18(40)11-9-17)39-27(45)21(15-23(41)42)37-26(44)20(7-3-4-12-31)36-25(43)19(32)6-5-13-35-30(33)34/h8-11,16,19-22,24,40H,3-7,12-15,31-32H2,1-2H3,(H,36,43)(H,37,44)(H,38,46)(H,39,45)(H,41,42)(H,47,48)(H4,33,34,35)/t19-,20-,21-,22-,24-/m0/s1

Upstream product

• 86060-98-2 Fmoc-L-Lys(Boc)-OPfp 
• 86060-87-9 Fmoc-Val-OPfp 
• 71989-38-3 Fmoc-Tyr(tBu)-OH 
• 86061-01-0 tert-butyl N-[(9H-fluoren-9-ylmethoxy)carbonyl]-1-pentafluorophenyl L-aspartate 
• 13734-41-3 t-Boc-L-valine 
• 80621-99-4 H-Val-Tyr-OBzl 
• 68858-20-8 Fmoc-Val-OH 
• 71989-14-5 Fmoc-(tBu)Asp-OH 
• 71989-26-9 Fmoc-Lys(tert-butoxycarbonyl) 
• 143824-77-5 N-α-(9-fluorenylmethyloxycarbonyl)-N-ω′,N-ω″-bis-tert-butyloxycarbonyl-L-argine 
• 13726-76-6 t-butyloxycarbonyl-L-arginine 
• 1544315-27-6 C₅₈H₇₇N₉O₁₃ 
• 16964-83-3 H-Lys(Z)-OBzl*TosOH 
• 158899-11-7 Nα-(9-fluorenylmethoxycarbonyl)-Nω,Nω'-bis(tert-butoxycarbonyl)-L-arginine 

Downstream Products

• 1099823-48-9 thymopentin ethyl ester 

Relevant articles and documents

SYSTEM AND METHOD FOR SOLUTION PHASE GAP PEPTIDE SYNTHESIS

Disclosed is a system and method for Fmoc/tBu solution-phase peptide synthesis including the development of a new benzyl-type GAP protecting group, and related uses thereto. This novel GAP protecting group is utilized in place of a polymer support, facilitating C to N Fmoc peptide synthesis without chromatography, recrystallization, or polymer supports. The GAP group can be added and removed in high yield.

Tetrahydro-β-carboline-3-carboxyl-thymopentin: A nano-conjugate for releasing pharmacophores to treat tumor and complications

To improve the therapeutic efficacy of cancer patients a novel conjugate of thymopentin (TP5) and (1S,3S)-1-methyl-tetrahydro-β-carboline-3-carboxylic acid (MTC) was presented. In water and mouse plasma MTCTP5 forms the nanoparticles of 14-139 nm in diameter, the suitable size for delivery in blood circulation. In mouse plasma MTCTP5 releases MTC, while in the presence of trypsin MTCTP5 releases MTC and TP5. On mouse and rat models the MTCTP5 dose dependently slows down the tumor growth, inhibits inflammatory response and blocks thrombosis. The anti-tumor activity as well as the anti-inflammation activity and anti-thrombotic activity of MTCTP5 are 100 fold and 10 fold higher than those of MTC, respectively, which are attributed to the fact that it down-regulates the plasma levels of TNF-α and IL-8 of the treated animals. The immunology enhancing activities in vitro and in vivo of MTCTP5 are similar to those of TP5, which is attributed to the fact that MTCTP5 up-regulates the plasma levels of IL-2 and CD4 as well as down-regulates the plasma level of CD8 of the treated animals. The plasma alanine transaminase, aspartate transaminase and creatinine assays indicate that MTCTP5 therapy does not injure the liver and the kidney of the animals. The survival time of MTCTP5 treated mice is significantly longer than that of TP5 treated mice.

GAP Peptide Synthesis through the Design of a GAP Protecting Group: An Fmoc/tBu Synthesis of Thymopentin Free from Polymers, Chromatography and Recrystallization

A novel method for Fmoc/tBu solution-phase peptide synthesis and the development of a new benzyl-type group-assisted purification (GAP) protecting group is reported. This GAP protecting group is utilized in place of a polymer support, facilitating C→N Fmoc peptide synthesis without chromatography or recrystallization. The GAP group can be added and removed in high yield, and was used to synthesize over 1 gram of the immunostimulant, thymopentin, in high overall yield (83 %) and purity (99 %). Fmoc/tBu solution-phase peptide synthesis and the development of a new benzyl-type group-assisted purification (GAP) protecting group is reported. This new GAP protecting group replaces a polymer support, facilitating C→N Fmoc peptide synthesis without chromatography or recrystallization. Over 1 gram of the immunostimulant, thymopentin, was synthesized in high overall yield (83 %) and purity (99 %).

Solvent-free peptide synthesis assisted by microwave irradiation: Environmentally benign synthesis of bioactive peptides

An efficient and facile, solvent-free peptide synthesis assisted by microwave irradiation, using DIC/HONB as the coupling reagent combination is reported. Key features of this original protocol are solvent-free synthesis, very short reaction time and scal

Membrane enhanced peptide synthesis

This communication reports a new technology platform that advantageously combines organic solvent nanofiltration (a newly emerging technology capable of molecular separations in organic solvents) with solution phase peptide synthesis - Membrane Enhanced Peptide Synthesis (MEPS).

Organic solvent nanofiltration: A new paradigm in peptide synthesis

Solid-phase synthesis is the dominant paradigm for peptide synthesis, used ubiquitously from discovery to production scale. However, the solid-phase approach produces coupling steps that may not be quantitative, introducing errors in amino acid sequences. It also entails an excess of reagents to overcome mass transfer limitations and restrictions on solvent, coupling chemistry, and protecting groups. Organic solvent nanofiltration (OSN) is a newly emerging technology capable of molecular separations in organic solvents. This contribution reports a new technology platform which advantageously combines OSN with solution-phase peptide synthesis, Membrane Enhanced Peptide Synthesis (MEPS). A first amino acid is linked to a soluble polyethylene glycol anchor. Through subsequent repeated coupling and deprotection steps, the peptide is extended to the desired length. The residual byproducts and excess reagents after each reaction are removed by diafiltration through a solvent-stable membrane which retains the peptide. Two pentapeptides are produced using this new technology. The purity of the peptides produced by MEPS is higher than that of peptides produced by solid-phase synthesis, under the same conditions. This illustrates clearly that MEPS benefits from the advantages of solution-phase synthesis, while avoiding the purification steps that have until now made solution-phase synthesis practically difficult.

Immunoactive peptides: VI. Synthesis of new analogs of thymopoietin

A new scheme for preparing a pentapeptide of thymopoietin (ArgLysAspValTyr, TP-5) is proposed, featuring a versatile combination of the maximal and minimal protection principles. The scheme was used to prepare the Gly2, Pro2, Ala3, and Arg2, Ala3 analogs of TP-5.

Amino acid protecting groups

This invention relates to compounds of the formula a compound of the formula STR1 wherein X is O, CR7 R8, S or NR9 wherein R7 and R8 are independently hydrogen, or lower alkyl, and R9 is lower alkyl; n is 0 or 1; R1 and R2 are independently hydrogen, lower alkyl, monoorganosilyl, diorganosilyl, triorganosilyl, halogen, aryl, or nitro; R3 is hydrogen, lower alkyl, monoorganosilyl, diorganosilyl, triorganosilyl, halogen, 9-fluorenylalkyl, cycloalkyl, aryl or aralkyl; R4 and R5 are independently hydrogen, lower alkyl, or aryl or one of R4 and R5 is 9-fluorenyl; R6 is H or COZ wherein Z is an amino acid, a peptide residue or a leaving group; and with the provisos that when n is 0 and R3 is hydrogen, R1 and R2 are not hydrogen, halogen or nitro; that when n is 0 and R3 is lower alkyl, R1 and R2 are not hydrogen; and that when X is O or CR7 R8 wherein R7 and R8 are H, that R1, R2, R3, R4, R5, and R6 are not all simultaneously H. The compounds of the present invention are useful in peptide synthesis as blocking or protecting groups for reactive groups. The present invention is also directed to a method of protecting a reactive group of an organic molecule during a reaction which modifies a portion of the molecule other than the protected group.

THE CONFORMATION OF THYMOPENTIN IN WATER. DISCRIMINATION BETWEEN TWO POSSIBLE &γ-TURNS BY A SIMPLE 13C-NMR PROCEDURE

Using of a simple, hydantoin scale utilizing procedure, we found that the conformational equilibrium of thymopentin (TP-5) in water is dominated by the folded conformation with a γ-turn (Φ=70 deg, Ψ=-72 deg) on the Asp3 residue.The mean solution conformation obtained from NMR data corresponds well with the computed minimum potential energy conformation of TP-5.The conformation found seems to be of importance for biological activity of TP-5.A new solid phase synthesis of TP-5 is also presented.

Cleavage of esters using carbonates and bicarbonates of alkali metals: Synthesis of thymopentin

A novel method for hydrolysis of primary esters using aqueous alkali carbonates or bicarbonates and an alcohol as cosolvent is described. Several peptide esters, including a Cbz-Arg-Lys(Cbz)-Asp(OBzl)-Val-Tyr-OBzl (sequence corresponding to the active site of thymic immunoregulatory hormone, thymopoietin), were hydrolyzed to demonstrate the utility of this method.