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1627676-59-8

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Structure–Activity Relationship Studies on (R)-PFI-2 Analogues as Inhibitors of Histone Lysine Methyltransferase SETD7
SETD7 is a histone H3K4 lysine methyltransferase involved in human gene regulation. Aberrant expression of SETD7 has been associated with various diseases, including cancer. Therefore, SETD7 is considered a good target for the development of new epigenetic drugs. To date, few selective small-molecule inhibitors have been reported that target SETD7, the most potent being (R)-PFI-2. Herein we report structure–activity relationship studies on (R)-PFI-2 and its analogues. A library of 29 structural analogues of (R)-PFI-2 was synthesized and evaluated for inhibition of recombinantly expressed human SETD7. The key interactions were found to be a salt bridge and a hydrogen bond formed between (R)-PFI-2′s NH2+ group and SETD7′s Asp256 and His252 residue, respectively.
Lenstra, Danny C.,Damen, Eddy,Leenders, Ruben G. G.,Blaauw, Richard H.,Rutjes, Floris P. J. T.,Wegert, Anita,Mecinovi?, Jasmin
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p. 1405 - 1413
(2018/07/29)

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Chemical Properties

Boiling Point: 642.7±65.0 °C(Predicted)
Density: 1.371±0.06 g/cm3(Predicted)
Solubility:≥50 mg/mL in DMSO; ≥1.51 mg/mL in H2O with gentle warming and ultrasonic; ≥8.12 mg/mL in EtOH
PKA: 8.95±0.20(Predicted)
PSA: 86.89000
LogP: 4.74060

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