5959-90-0

Usage

Uses

Used in Pharmaceutical Applications:
Adenosine 5'-triphosphate 5'-adenosine is used as a therapeutic agent for treating pathological calcification and ossification. It helps in the regulation of calcium homeostasis and prevents the abnormal deposition of calcium salts in soft tissues, which can lead to various diseases and complications.
Used in Drug Discovery:
Ap5A is utilized in the identification of potent inhibitors for chromodomain-helicase-DNA-binding protein 1 (CHD1). CHD1 is a chromatin remodeling enzyme that plays a role in gene regulation and has been implicated in various diseases, including cancer. By using Ap5A as a starting point, researchers can develop novel inhibitors that target CHD1, potentially leading to the development of new therapeutic strategies for these diseases.
Used in Research and Development:
Adenosine 5'-triphosphate 5'-adenosine is also used as a research tool in the study of cellular signaling pathways and the development of new drugs targeting various diseases. Its unique properties and ability to interact with multiple proteins make it an invaluable compound for understanding the complex mechanisms underlying cellular processes and for designing targeted therapies.

InChI:InChI=1/2C10H13N5O4.3H3O4P/c2*11-8-5-9(13-2-12-8)15(3-14-5)10-7(18)6(17)4(1-16)19-10;3*1-5(2,3)4/h2*2-4,6-7,10,16-18H,1H2,(H2,11,12,13);3*(H3,1,2,3,4)/t2*4-,6-,7-,10-;;;/m11.../s1

Upstream product

• 61-19-8 5'-adenosine monophosphate 
• 58-64-0 adenosine 5'-diphosphate 
• 56-65-5 ATP 
• 35985-27-4 lysyl adenylate 
• 20816-58-4 adenosine 5'-phosphorimidazolide 
• 4691-96-7 adenosine 5'-triphosphate sodium salt 
• 1350980-53-8 C₂₆H₄₁N₁₀O₁₅P₃S 

Downstream Products

• 60-92-4 cAMP 
• 61-19-8 5'-adenosine monophosphate 
• 58-64-0 adenosine 5'-diphosphate 
• 66224-66-6 adenine 
• 4578-31-8 adenosine-5'-monophosphate disodium salt 

Relevant academic research and scientific papers

Isolation and identification of diadenosine 5′,5?-P 1,P4-tetraphosphate binding proteins using magnetic bio-panning

We report the development of a synthetic, biotin-conjugated diadenosine tetraphosphate (Ap4A)-'molecular hook' attached to magnetic beads enabling the isolation of Ap4A-binding proteins from bacterial cells or mammalian tissue lysates. Characterisation and identification of isolated binding proteins is performed sequentially by mass spectrometry. The observation of positive controls suggests that these newly observed proteins are putative Ap4A-binding partners, and we have expectations that others can be found with further technical improvements in our methods.

Solid-phase synthesis of symmetrical 5′,5′-dinucleoside mono-, di-, tri-, and tetraphosphodiesters

(Chemical Equation Presented) Four classes of phosphitylating reagents were subjected to reactions with aminomethyl polystyrene resin-bound p-acetoxybenzyl alcohol to yield the corresponding polymer-bound mono-, di-, tri-, and tetraphosphitylating reagents. The solid-phase reagents were reacted with unprotected nucleosides (e.g., thymidine, adenosine, 3′-azido-3′- deoxythymidine, cytidine, or inosine) in the presence of 5-(ethylthio)-1H- tetrazole. Polymer-bound nucleosides underwent oxidation with fert-butyl hydroperoxide, deprotection of cyanoethoxy groups with DBU, and the acidic cleavage, respectively, to afford 5′,5′-dinucleoside mono-, di-, tri-, and tetraphosphodiesters in 59-78% yield.

NEW USES OF DINUCLEOTIDE POLYPHOSPHATE DERIVATIVES

The present invention provides the use of analogues and derivatives of dinucleoside polyphosphates with formula (I) or a pharmaceutically acceptable salt thereof, in the manufacture of a medicament for use in one or more of: the treatment of ischemia, inducing ischemic tolerance, modulating cerebral ischemia, to delay the onset of a hypoxic depolarisation stage when ischemic events are initiated; as a neurological protection agent; as a tissue protection agent; the treatment of pain; and the treatment of inflammation, wherein X, is selected from wherein X1 and X2 are independently selected from H, Cl, Br and F; each Y is independently selected from S and O; each Z is independently selected from -CX3X4-,-NH-,-O- ; wherein X3 and X4 are selected from H, CI, Br and F; B1 and B2 are independently selected from adenine, guanine, xanthine, thymine, uracil, cytosine and inosine; S1 and S2 are independently selected from ribose, open chain ribose, 2'-deoxyribose, 3'deoxyribose and arabinofuranoside. V is selected from 0, 1 , 2, 3, 4 and 5; W is selected from 0, 1 , 2, 3, 4 and 5; and V plus W is an integer from 2 to 6.

Engineering human FHIT, a diadenosine triphosphate hydrolase, into an efficient dinucleoside polyphosphate synthase

The putative human tumor suppressor gene FHIT encodes Fhit, the fragile histidine triad protein. Fhit is thought to participate in a signal transduction pathway involving dinucleoside polyphosphates. Fhit catalyzes the Mg2+-dependent hydrolysis of P1-5′-O-adenosine-P3-5′-O-adenosine triphosphate (Ap3A) to AMP and MgADP. Mutation of His96 to glycine disables Fhit as a catalyst for the hydrolysis of phosphoanhydrides such as Ap3A. However, the mutated enzyme H96G-Fhit efficiently catalyzes the synthesis of phosphoanhydride bonds in reactions of nucleoside-5′-phosphimidazolides with nucleoside di- and triphosphates. H96G-Fhit can be employed in the synthesis of a wide range of dinucleoside tri- and tetraphosphates. We here describe the use of H96G-Fhit to catalyze the synthesis of Ap3A, Ap3C, Ap3G, Ap3T, Ap3U, Cp3U, Tp3U, dAp3U, Ap4A, Ap4U, and the fluorescent Ap4etheno-C. Copyright

Synthesis and reactions of nucleoside 5'-diphosphate imidazolide. A nonenzymatic capping agent for 5'-monophosphorylated oligoribonucleotides in aqueous solution

We have synthesized adenosine and 7-methylguanosine 5'-diphosphate imidazolides from imidazole and the corresponding nucleoside 5'-diphosphates. The phosphorimidazolide bond of the compounds was susceptible to hydrolysis and hydrolyzed gradually in neutral aqueous solution, but it was more stable than that of the corresponding imidazolides of nucleoside 5'-monophosphate. The 7-methylguanosine 5'-diphosphate imidazolide reacted with guanosine 5'- monophosphate or 5' monophosphorylated oligoribonucleotides in neutral aqueous solution in the presence of an Mn2- ion catalyst converting to the cap portion of mRNA or the capped m7Gppp-oligoribonucleotides in substantial yields. The condensation reaction of adenosine 5'-diphosphate imidazolide with adenosine 5'-monophosphate took place similarly in neutral aqueous solution by a divalent metal ion-catalyst such as Mg2+ or Mn2+, yielding diadenosine 5',5'-triphosphate.

Characterisation of stress protein LysU. Enzymic synthesis of diadenosine 5′,5?-P1,P4-tetraphosphate (Ap4A) analogues by LysU

The stress protein LysU (lysyl tRNA synthetase) has been purified from a recombinant strain of Escherichia coli expressing the plasmid pXLys5, and kinetically characterised. Preparative syntheses of analogues of the biologically important molecule diadenosine 5′,5?-P1,P4-tetraphosphate (Ap4A) are then achieved in good yield by enzyme catalysis, using purified LysU.

One-Pot Synthesis of α,γ-Dinucleoside 5'-Triphosphates, G5'pppG and A5'pppA, Using S,S'-Bis(4-chlorophenyl)phosphorodithioate

S,S'-Bis(4-chlorophenyl) phosphorodithioate was useful for the synthesis of α,γ-dinucleoside 5'-triphosphates, G5'pppG and A5'pppA starting from the corresponding unprotected nucleoside 5'-phosphates under neutral conditions. G5'pppG was used for the synthesis of m7G5'pppG by means of the N7-methylation of one of two guanine moieties of G5'pppG.

Facile synthesis of nucleotides containing polyphosphates by Mn(II) and Cd(II) ion-catalyzed pyrophosphate bond formation in aqueous solution

Mn2+ and Cd2+ catalyzed pyrophosphate bond formation from adenosine-5'-phosphorimidazolide and nucleotides or phosphates in neutral aqueous solution, giving nucleotides containing polyphosphates.

Facile and Selective Synthesis of Diadenosine Polyphosphates through Catalysis by Leucyl t-RNA Synthetase Coupled with ATP Regeneration

Leucyl t-RNA synthetase from a thermophilic bacterium, Bacillus stearothermophillus, effectively catalyzed the synthesis of p1,p4-di(adenosine 5'-)tetraphosphate (Ap4A), p1,p5-di(adenosine 5'-)pentaphosphate (Ap5A) and adenosine 5'-tetraphosphate (p4A).In particular, when the reaction was coupled with an ATP recycling system involving thermostable acetate kinase and adenylate kinase, Ap4A and Ap5A were produced selectively in high yields.This reaction is selective, gives high yields and does not require protection of the functional groups of nucleotides, and also it can be carried out in an aqueous solution.This method is superior to the conventional organic synthesis and provides a practical means of the synthesizing diadenosine polyphosphates (ApnA), biologically important compounds.