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, F. González-Nilo

Resultado de la investigación: Article

9 Citas (Scopus)

Resumen

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.

Idioma originalEnglish
Páginas (desde-hasta)19001-19011
Número de páginas11
PublicaciónPhysical Chemistry Chemical Physics
Volumen17
N.º29
DOI
EstadoPublished - 7 ago 2015

Huella dactilar

Apoferritins
Dendrimers
dendrimers
Ferritins
inhibitors
Iron
iron
interactions
homeostasis
entry
amines
electrostatics
molecular dynamics
proteins
cavities
Molecular Dynamics Simulation
PAMAM Starburst
PAMAM-G4
Static Electricity
Amines

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Physics and Astronomy(all)
  • Medicine(all)

Citar esto

Camarada, M. B. ; Márquez-Miranda, V. ; Araya-Durán, I. ; Yévenes, A. ; González-Nilo, F. / PAMAM G4 dendrimers as inhibitors of the iron storage properties of human L-chain ferritin. En: Physical Chemistry Chemical Physics. 2015 ; Vol. 17, N.º 29. pp. 19001-19011.
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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.",
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PAMAM G4 dendrimers as inhibitors of the iron storage properties of human L-chain ferritin. / Camarada, M. B.; Márquez-Miranda, V.; Araya-Durán, I.; Yévenes, A.; González-Nilo, F.

En: Physical Chemistry Chemical Physics, Vol. 17, N.º 29, 07.08.2015, p. 19001-19011.

Resultado de la investigación: Article

TY - JOUR

T1 - PAMAM G4 dendrimers as inhibitors of the iron storage properties of human L-chain ferritin

AU - Camarada, M. B.

AU - Márquez-Miranda, V.

AU - Araya-Durán, I.

AU - Yévenes, A.

AU - González-Nilo, F.

PY - 2015/8/7

Y1 - 2015/8/7

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AB - 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.

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