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L-Adenosine Sale

(Synonyms: L-腺苷) 目录号 : GC66645

L-Adenosine 是一种代谢稳定的对映异构体类似物,也是一种潜在的探针。L-Adenosine 具有弱抑制性腺苷脱氨酶 (ADA) 活性,Ki 值为 385 μM。L-Adenosine 可用于腺苷摄取和积累的研究。

L-Adenosine Chemical Structure

Cas No.:3080-29-3

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产品描述

L-Adenosine is a metabolically stable enantiomeric analog and also is a potential probe. L-Adenosine has weakly inhibitory adenosine deaminase (ADA) activity with an Ki value of 385 μM. L-Adenosine can be used for the research of adenosine uptake and accumulation[1].

L-Adenosine (10-10,000 μM) weakly inhibits rat brain adenosine deaminase (ADA) activity with an Ki value of 385 μM[1].

[1]. J G Gu, et al. L-[3H]adenosine, a new metabolically stable enantiomeric probe for adenosine transport systems in rat brain synaptoneurosomes. J Neurochem. 1991 Feb;56(2):548-52.

Chemical Properties

Cas No. 3080-29-3 SDF Download SDF
别名 L-腺苷
分子式 C10H13N5O4 分子量 267.24
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Research Update

Novel L-Adenosine analogs as cardioprotective agents

Bioorg Med Chem 2009 Jul 15;17(14):5347-52.PMID:19502065DOI:10.1016/j.bmc.2008.12.011.

Two l-nucleosides, l-3'-amino-3'-deoxy-N(6)-dimethyladenosine (l-3'-ADMdA) 1, previously synthesized in our laboratory, and the novel l-3'-amino-3'-deoxy-N(6)-methyladenosine-5'-N-methyluronamide (l-3'-AM-MECA) 2 were evaluated in an ischemia/reperfusion model on Langendorff perfused mouse heart. l-3'-ADMdA 1 was found to enhance functional recovery from ischemia (32.2+/-3.7cm H(2)O/s % rate pressure product, compared to 21.3+/-1.4 for the control and 30.7+/-3.4 for adenosine) and increase the time to onset of ischemic contracture (14.5+/-0.9min, compared to 10.5+/-1.0min for the control and 13.6+/-0.6min for adenosine) comparable to adenosine. Consistent with the functional recovery data, decreased infarction area was seen in the case of 1 (19.1+/-8.4, compared to 40.5+/-7.2% for the control and 11.5+/-2.1% for adenosine). In contrast, l-3'-AM-MECA 2 did not show significant functional recovery, increased onset of contracture, nor decreased infarction area compared to control. Unlike adenosine, neither 1 nor 2 induced cardiac standstill in mouse heart.

Are L-Adenosine and its derivatives substrates for S-adenosyl-L-homocysteine hydrolase?

J Med Chem 2005 May 19;48(10):3649-53.PMID:15887973DOI:10.1021/jm0490484.

Moffatt oxidation of 2',3'-O-isopropylidene-L-adenosine and treatment of the resulting crude 5'-aldehyde with hydroxylamine followed by deprotection gave L-Adenosine 5'-carboxaldehyde oximes, whose enantiomers are known to be potent inhibitors of S-adenosyl-L-homocysteine (AdoHcy) hydrolase. The L-Adenosine and its 5'-aldehyde oxime derivatives were found to be inactive as inhibitors of AdoHcy hydrolase. Docking calculations showed that binding of L-Adenosine to AdoHcy hydrolase is weaker (higher energy) and less specific (larger number of clusters) compared to D-Ado.

L-[3H]adenosine, a new metabolically stable enantiomeric probe for adenosine transport systems in rat brain synaptoneurosomes

J Neurochem 1991 Feb;56(2):548-52.PMID:1988556DOI:10.1111/j.1471-4159.1991.tb08184.x.

The stereoenantimers D-[3H]adenosine and L-[3H]adenosine were used to study adenosine accumulation in rat cerebral cortical synaptoneurosomes. L-Adenosine very weakly inhibited rat brain adenosine deaminase (ADA) activity with a Ki value of 385 microM. It did not inhibit rat brain adenosine kinase (AK) activity, nor was it utilized as a substrate for either ADA or AK. The rate constants (fmol/mg of protein/s) for L-[3H]adenosine accumulation measured in assays where transport was stopped either with inhibitor-stop centrifugation or with rapid filtration methods were 82 +/- 14 and 75 +/- 10, respectively. Using the filtration method, the rates of L-[3H]adenosine accumulation were not significantly different from the value of 105 +/- 15 fmol/mg of protein/s measured for D-[3H]adenosine transport. Unlabeled D-adenosine and nitrobenzylthiolnosine, both at a concentration of 100 microM, reduced the levels and rates of L-[3H]adenosine accumulation by greater than 44%. These findings suggest that L-Adenosine, a metabolically stable enantiomeric analog, and the naturally occurring D-adenosine are both taken up by rat brain synaptoneurosomes by similar processes, and as such L-Adenosine may represent an important new probe with which adenosine uptake may be studied.

Involvement of bidirectional adenosine transporters in the release of L-[3H]adenosine from rat brain synaptosomal preparations

J Neurochem 1995 May;64(5):2105-10.PMID:7722493DOI:10.1046/j.1471-4159.1995.64052105.x.

Adenosine transport inhibitors as enhancers of extracellular levels of endogenous adenosine would, presumably, only be effective if, for example, (1) the inhibitors block influx to a greater degree than efflux (release) of intracellular adenosine or (2) the inhibitors block equally well the influx and efflux of adenosine, but significant amounts of adenosine are formed as a result of dephosphorylation of released adenine nucleotides. Limited information is available regarding the directional symmetry of adenosine transporters in neural cells. Using rat brain crude P2 synaptosomal preparations preloaded with L-[3H]adenosine, our objectives here were to determine (1) if L-[3H]adenosine, a substrate for adenosine transporters that is more metabolically stable than physiological D-adenosine, was being released from synaptosomal preparations, (2) the optimal conditions necessary to observe the release, and (3) the degree to which this release was mediated by efflux through bidirectional nucleoside transporters. L-[3H]Adenosine release was found to be concentration and time dependent, temperature sensitive, and linear with synaptosomal protein. L-[3H]Adenosine release was inhibited dose-dependently by dipyridamole, nitrobenzylthioinosine, and dilazep; at concentrations of 100 microM inhibition was at least 40% for dipyridamole, 52% for nitrobenzylthioinosine, and 49% for dilazep. After loading with L-[3H]adenosine alone or I-[3H]adenosine plus unlabeled L-Adenosine, D-adenosine, or uridine, L-[3H]adenosine release was inhibited 42% by L-Adenosine, 69% by uridine, and 81% by D-adenosine.(ABSTRACT TRUNCATED AT 250 WORDS)

Mirror-image RNA that binds D-adenosine

Nat Biotechnol 1996 Sep;14(9):1112-5.PMID:9631061DOI:10.1038/nbt0996-1112.

A 58-mer L-RNA ligand that binds to naturally occurring D-adenosine with a dissociation constant of 1.7 microM in solution was identified from a combinatorial library employing mirror-design. The corresponding D-RNA ligand shows identical binding affinity to L-Adenosine. Reciprocal chiral specificity was also evident from ligand discrimination; the binding affinity of the L-RNA ligand for D-adenosine was 9000-fold greater than its affinity for L-Adenosine and vice versa. While the D-RNA ligand was rapidly degraded in human serum, the L-RNA ligand displayed an extraordinary stability. This indicates the potential application of specifically designed L-RNA ligands as stable monoclonal antibody analogues and the development of highly stable L-ribozymes.