Phthalazine PDE4 inhibitors. Part 3: The synthesis and in vitro evaluation of derivatives with a hydrogen bond acceptor

Mauro Napoletano, Gabriele Norcini, Franco Pellacini, Francesco Marchini, Gabriele Morazzoni, Raimondo Fattori, Pierpaolo Ferlenga, Lorenzo Pradella

Research output: Contribution to journalArticle

Abstract

This communication describes the synthesis and in vitro evaluation of a novel and potent series of phthalazine phosphodiesterase type (IV) (PDE4) inhibitors. The interaction with two distinct polar binding sites allowed us to eliminate the cyclopentyloxy substitution from rolipram-like analogues.

Original languageEnglish
Pages (from-to)5-8
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume12
Issue number1
DOIs
Publication statusPublished - Jan 7 2002

Fingerprint

Type 4 Cyclic Nucleotide Phosphodiesterase
Phosphodiesterase 4 Inhibitors
Rolipram
Hydrogen
Hydrogen bonds
Substitution reactions
Binding Sites
Derivatives
Communication
phthalazine
In Vitro Techniques

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry
  • Drug Discovery
  • Pharmaceutical Science

Cite this

Phthalazine PDE4 inhibitors. Part 3 : The synthesis and in vitro evaluation of derivatives with a hydrogen bond acceptor. / Napoletano, Mauro; Norcini, Gabriele; Pellacini, Franco; Marchini, Francesco; Morazzoni, Gabriele; Fattori, Raimondo; Ferlenga, Pierpaolo; Pradella, Lorenzo.

In: Bioorganic and Medicinal Chemistry Letters, Vol. 12, No. 1, 07.01.2002, p. 5-8.

Research output: Contribution to journalArticle

Napoletano, M, Norcini, G, Pellacini, F, Marchini, F, Morazzoni, G, Fattori, R, Ferlenga, P & Pradella, L 2002, 'Phthalazine PDE4 inhibitors. Part 3: The synthesis and in vitro evaluation of derivatives with a hydrogen bond acceptor', Bioorganic and Medicinal Chemistry Letters, vol. 12, no. 1, pp. 5-8. https://doi.org/10.1016/S0960-894X(01)00668-0
Napoletano, Mauro ; Norcini, Gabriele ; Pellacini, Franco ; Marchini, Francesco ; Morazzoni, Gabriele ; Fattori, Raimondo ; Ferlenga, Pierpaolo ; Pradella, Lorenzo. / Phthalazine PDE4 inhibitors. Part 3 : The synthesis and in vitro evaluation of derivatives with a hydrogen bond acceptor. In: Bioorganic and Medicinal Chemistry Letters. 2002 ; Vol. 12, No. 1. pp. 5-8.
@article{ee226d52d85b45d8a30462be14073f3b,
title = "Phthalazine PDE4 inhibitors. Part 3: The synthesis and in vitro evaluation of derivatives with a hydrogen bond acceptor",
abstract = "This communication describes the synthesis and in vitro evaluation of a novel and potent series of phthalazine phosphodiesterase type (IV) (PDE4) inhibitors. The interaction with two distinct polar binding sites allowed us to eliminate the cyclopentyloxy substitution from rolipram-like analogues.",
author = "Mauro Napoletano and Gabriele Norcini and Franco Pellacini and Francesco Marchini and Gabriele Morazzoni and Raimondo Fattori and Pierpaolo Ferlenga and Lorenzo Pradella",
year = "2002",
month = "1",
day = "7",
doi = "10.1016/S0960-894X(01)00668-0",
language = "English",
volume = "12",
pages = "5--8",
journal = "Bioorganic and Medicinal Chemistry Letters",
issn = "0960-894X",
publisher = "Elsevier Limited",
number = "1",

}

TY - JOUR

T1 - Phthalazine PDE4 inhibitors. Part 3

T2 - The synthesis and in vitro evaluation of derivatives with a hydrogen bond acceptor

AU - Napoletano, Mauro

AU - Norcini, Gabriele

AU - Pellacini, Franco

AU - Marchini, Francesco

AU - Morazzoni, Gabriele

AU - Fattori, Raimondo

AU - Ferlenga, Pierpaolo

AU - Pradella, Lorenzo

PY - 2002/1/7

Y1 - 2002/1/7

N2 - This communication describes the synthesis and in vitro evaluation of a novel and potent series of phthalazine phosphodiesterase type (IV) (PDE4) inhibitors. The interaction with two distinct polar binding sites allowed us to eliminate the cyclopentyloxy substitution from rolipram-like analogues.

AB - This communication describes the synthesis and in vitro evaluation of a novel and potent series of phthalazine phosphodiesterase type (IV) (PDE4) inhibitors. The interaction with two distinct polar binding sites allowed us to eliminate the cyclopentyloxy substitution from rolipram-like analogues.

UR - http://www.scopus.com/inward/record.url?scp=0037033177&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037033177&partnerID=8YFLogxK

U2 - 10.1016/S0960-894X(01)00668-0

DO - 10.1016/S0960-894X(01)00668-0

M3 - Article

C2 - 11738561

AN - SCOPUS:0037033177

VL - 12

SP - 5

EP - 8

JO - Bioorganic and Medicinal Chemistry Letters

JF - Bioorganic and Medicinal Chemistry Letters

SN - 0960-894X

IS - 1

ER -