Research output: Contribution to journal › Article › peer-review
A versatile strategy for the design and synthesis of novel ADP conjugates and their evaluation as potential poly(ADP-ribose) polymerase 1 inhibitors. / Sherstyuk, Yuliya V.; Zakharenko, Alexandra L.; Kutuzov, Mikhail M. et al.
In: Molecular Diversity, Vol. 21, No. 1, 01.02.2017, p. 101-113.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - A versatile strategy for the design and synthesis of novel ADP conjugates and their evaluation as potential poly(ADP-ribose) polymerase 1 inhibitors
AU - Sherstyuk, Yuliya V.
AU - Zakharenko, Alexandra L.
AU - Kutuzov, Mikhail M.
AU - Chalova, Polina V.
AU - Sukhanova, Maria V.
AU - Lavrik, Olga I.
AU - Silnikov, Vladimir N.
AU - Abramova, Tatyana V.
N1 - Publisher Copyright: © 2016, Springer International Publishing Switzerland.
PY - 2017/2/1
Y1 - 2017/2/1
N2 - Abstract: A versatile strategy for the synthesis of NAD + mimetics was developed, involving an efficient pyrophosphate linkage formation in key conjugates containing a functional amino group which acts as useful reactive anchor for further derivatization. These NAD + mimetics consist of ADP conjugated through a diphosphate chain to an extended aliphatic linker bearing an aromatic acid residue. A number of conjugates containing aromatic carboxylic acids were found to inhibit poly(ADP-ribose) synthesis catalyzed by poly(ADP-ribose) polymerase-1 (PARP-1). A new class of potential PARP-1 inhibitors mimicking NAD +, a substrate in the PARP-1 catalyzed reaction, was proposed.
AB - Abstract: A versatile strategy for the synthesis of NAD + mimetics was developed, involving an efficient pyrophosphate linkage formation in key conjugates containing a functional amino group which acts as useful reactive anchor for further derivatization. These NAD + mimetics consist of ADP conjugated through a diphosphate chain to an extended aliphatic linker bearing an aromatic acid residue. A number of conjugates containing aromatic carboxylic acids were found to inhibit poly(ADP-ribose) synthesis catalyzed by poly(ADP-ribose) polymerase-1 (PARP-1). A new class of potential PARP-1 inhibitors mimicking NAD +, a substrate in the PARP-1 catalyzed reaction, was proposed.
KW - NAD analogues
KW - PARP inhibitors
KW - PARP-1
KW - Pyrophosphate synthesis
KW - NAD/chemistry
KW - Poly (ADP-Ribose) Polymerase-1/antagonists & inhibitors
KW - Chemistry Techniques, Synthetic
KW - Biomimetic Materials/chemical synthesis
KW - Drug Design
KW - Adenosine Diphosphate/chemistry
KW - Enzyme Inhibitors/chemical synthesis
KW - ACID
KW - CHROMATIN
KW - NICOTINAMIDE
KW - PROBING BINDING REQUIREMENTS
KW - STRUCTURAL-ANALYSIS
KW - FUNCTIONALIZATION
KW - REPAIR
KW - DNA
KW - NAD ANALOGS
KW - NAD(+) analogues
KW - PARP INHIBITORS
UR - http://www.scopus.com/inward/record.url?scp=84988723483&partnerID=8YFLogxK
U2 - 10.1007/s11030-016-9703-x
DO - 10.1007/s11030-016-9703-x
M3 - Article
C2 - 27677737
AN - SCOPUS:84988723483
VL - 21
SP - 101
EP - 113
JO - Molecular Diversity
JF - Molecular Diversity
SN - 1381-1991
IS - 1
ER -
ID: 8680829