81129-37-5 Usage
Classification
Purine derivative
Function
Potent and selective antagonist of adenosine A1 receptors
Role in Neurotransmission
Regulates neurotransmitter release and mediates the effects of adenosine
Therapeutic Applications
Parkinson's disease, ischemia, and neurodegenerative disorders
Additional Applications
Treatment of asthma and chronic obstructive pulmonary disease (due to bronchodilator properties)
Other Effects
Anti-inflammatory and anti-oxidant properties
Potential
Promising candidate for the development of new drugs for a variety of medical conditions
Check Digit Verification of cas no
The CAS Registry Mumber 81129-37-5 includes 8 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 5 digits, 8,1,1,2 and 9 respectively; the second part has 2 digits, 3 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 81129-37:
(7*8)+(6*1)+(5*1)+(4*2)+(3*9)+(2*3)+(1*7)=115
115 % 10 = 5
So 81129-37-5 is a valid CAS Registry Number.
InChI:InChI=1/C15H27N4O2/c1-4-5-6-11(2)19(7-12(3)21)10-18-14-13(8-20)16-9-17-15(14)19/h9-13,20-21H,4-8H2,1-3H3,(H,16,17)/q+1/t11-,12+,13+,19?/m1/s1
81129-37-5Relevant articles and documents
Inhibitors of adenosine deaminase. Studies in combining high-affinity enzyme-binding structural units. erythro-1,6-Dihydro-6-(hydroxymethyl)-9-(2-hydroxy-3-nonyl)purine and erythro-9-(2-hydroxy-3-nonyl)purine.
Woo,Baker
, p. 603 - 605 (2007/10/02)
erythro-1,6-Dihydro-6-(hydroxymethyl)-9-(2-hydroxy-3-nonyl)purine (4) was synthesized as a potential adenosine deaminase inhibitor, which combines in a single molecule two structural moieties, each of which possesses high affinity to a different region of the enzyme, the catalytic region and an auxiliary binding region which is specific for erythro-9-(2-hydroxy-3-nonyl)adenine (1). The potency of 4 (Ki = 1.2 x 10(-5) M) is about one-seventeenth that of erythro-9-(2-hydroxy-3-nonyl)purine (2; Ki = 6.8 x 10(-7) M), which contains only one high-affinity moiety. The mutually interfering rather than reinforcing effects of the two moieties may indicate that lack of simultaneous binding and thus provide insight into the relative geometry of the two binding regions of the enzyme.
