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Issue 29, 2015
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PAMAM G4 dendrimers as inhibitors of the iron storage properties of human L-chain ferritin

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Abstract

Cationic dendrimers, such as PAMAM, are known to be positively charged at neutral pH allowing their unspecific interaction with proteins and other cellular components. Especially, ferritin, which has an important role in iron homeostasis, presents a negative electrostatic potential at the 3-fold channel. This channel is important in the functionality of ferritin because it allows the iron entry into its inner cavity. In this way, the interaction between the protonated terminal amines of the dendrimer and the negatively charged 3-fold channels of ferritin is expected. Experimental measurements demonstrated that PAMAM G4 inhibits the iron storage properties of L-chain human ferritin (L-Ftn). Molecular dynamics simulations have been used to analyze the specific interaction between PAMAM G4 and L-Ftn. Results show that PAMAM G4 effectively interacts with the 3-fold channels of L-Ftn, suggesting that this interaction is responsible for the inhibition of the iron storage properties of L-Ftn.

Graphical abstract: PAMAM G4 dendrimers as inhibitors of the iron storage properties of human L-chain ferritin

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Supplementary files

Article information


Submitted
04 May 2015
Accepted
21 Jun 2015
First published
24 Jun 2015

Phys. Chem. Chem. Phys., 2015,17, 19001-19011
Article type
Paper
Author version available

PAMAM G4 dendrimers as inhibitors of the iron storage properties of human L-chain ferritin

M. B. Camarada, V. Márquez-Miranda, I. Araya-Durán, A. Yévenes and F. González-Nilo, Phys. Chem. Chem. Phys., 2015, 17, 19001
DOI: 10.1039/C5CP02594J

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