Inhibition of polyamine and spermine oxidases by polyamine analogues

The FEBS Journal
Marzia BianchiAlessandra Cona

Abstract

Polyamine oxidase (PAO) and spermine oxidase (SMO) are involved in the catabolism of polyamines--basic regulators of cell growth and proliferation. The discovery of selective inhibitors of PAO and SMO represents an important tool in studying the involvement of these enzymes in polyamine homeostasis and a starting point for the development of novel antineoplastic drugs. Here, a comparative study on murine PAO (mPAO) and SMO (mSMO) inhibition by the polyamine analogues 1,8-diaminooctane, 1,12-diaminododecane, N-prenylagmatine (G3), guazatine and N,N1-bis(2,3-butadienyl)-1,4-butanediamine (MDL72527) is reported. Interestingly, 1,12-Diaminododecane and G3 behave as specific inhibitors of mPAO, values of K(i) for mPAO inhibition being lower than those for mSMO inactivation by several orders of magnitude. The analysis of molecular models of mPAO and mSMO indicates a significant reduction of the hydrophobic pocket located in maize PAO (MPAO) at the wider catalytic tunnel opening. This observation provides a rationale to explain the lower affinity displayed by G3, guazatine and MDL72527 for mPAO and mSMO as compared to MPAO. The different behaviour displayed by 1,12-diaminododecane towards mPAO and mSMO reveals the occurrence of basic ...Continue Reading

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Citations

Jul 6, 2013·Journal of Molecular Evolution·Manuela CervelliPaolo Mariottini
Aug 23, 2011·Amino Acids·Bonaiuto EmanuelaMaria Luisa Di Paolo
Aug 3, 2011·Amino Acids·Manuela CervelliPaolo Mariottini
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Jan 23, 2019·BMC Evolutionary Biology·Cesar Daniel BordenaveAndrés Alberto Rodríguez
Feb 24, 2021·Journal of Medicinal Chemistry·Xing-Jie DaiHong-Min Liu

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