Poly(amidoamine) dendrimer-methotrexate conjugates: the mechanism of interaction with folate binding protein

Mol Pharm. 2014 Nov 3;11(11):4049-58. doi: 10.1021/mp500608s. Epub 2014 Oct 1.

Abstract

Generation 5 poly(amidoamine) (G5 PAMAM) methotrexate (MTX) conjugates employing two small molecular linkers, G5-(COG-MTX)n, G5-(MFCO-MTX)n were prepared along with the conjugates of the G5-G5 (D) dimer, D-(COG-MTX)n, D-(MFCO-MTX)n. The monomer G5-(COG-MTX)n conjugates exhibited only a weak, rapidly reversible binding to folate binding protein (FBP) consistent with monovalent MTX binding. The D-(COG-MTX)n conjugates exhibited a slow onset, tight-binding mechanism in which the MTX first binds to the FBP, inducing protein structural rearrangement, followed by polymer-protein van der Waals interactions leading to tight-binding. The extent of irreversible binding is dependent on total MTX concentration and no evidence of multivalent MTX binding was observed.

Keywords: PAMAM dendrimer; methotrexate; multivalent binding; polymer/protein interactions.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Calorimetry
  • DNA Helicases / metabolism*
  • DNA-Binding Proteins / metabolism*
  • Dendrimers / chemistry*
  • Dendrimers / metabolism*
  • Humans
  • Methotrexate / chemistry*
  • Methotrexate / metabolism
  • Nuclear Magnetic Resonance, Biomolecular
  • Polyamines / chemistry*
  • Polyamines / metabolism
  • RNA-Binding Proteins
  • Surface Plasmon Resonance

Substances

  • DNA-Binding Proteins
  • Dendrimers
  • FUBP1 protein, human
  • Poly(amidoamine)
  • Polyamines
  • RNA-Binding Proteins
  • DNA Helicases
  • Methotrexate