Folate-binding protein self-aggregation drives agglomeration of folic acid targeted iron oxide nanoparticles
Junjie Chen, Sarah Klem, Alexis K. Jones, Bradford Orr, Mark M. Banaszak Holl
Folate-conjugated nanomaterials have been widely investigated for drug and imaging-agent delivery. In this work, two folic acid (FA) conjugated iron oxide particles (IOP), a ∼40 nm diameter FA-IOP and a ∼450 nm diameter FA-IOP(FA-SeraMag), were synthesized. Both particles aggregated in the presence of serum folate-binding protein (FBP) at physiological concentration and buffer conditions. Mixing 0.01% w/w FA-conjugated iron oxide particles with FBP-induced agglomeration generated an average hydro-dynamic particle diameter of 3800 ± 1100 nm for ∼40 nm FA-IOP and 4030 ± 1100 nm for FA-SeraMag as measured by dynamic light scattering (DLS). The presence of excess human serum albumin (HSA) (600 μM) did not prevent agglomeration of the ∼40 nm FA-IOP; however, it did inhibit agglomeration of FA-SeraMag. Atomic force microscopy measurement provided additional insight into particle morphology with the detection of individual particles in the agglomerate. This behavior is an example of a triggered cascade. A protein structural change is induced by FA binding, and the structural change favors aggregation of the ∼4 nm diameter FBPs on the particle surface; this further triggers the agglomeration of both the ∼40 and ∼450 nm diameter IOPs.
Bioconjugate Chemistry
https://doi.org/10.1021/acs.bioconjchem.6b00526
Published - 1 Jan 2017
Chen, J., Klem, S., Jones, A. K., Orr, B., & Holl, M. M. B. (2017). Folate-binding protein self-aggregation drives agglomeration of folic acid targeted iron oxide nanoparticles. Bioconjugate Chemistry, 28(1), 81-87. https://doi.org/10.1021/acs.bioconjchem.6b00526
Chen, Junjie ; Klem, Sarah ; Jones, Alexis K. ; Orr, Bradford ; Holl, Mark M. Banaszak. / Folate-binding protein self-aggregation drives agglomeration of folic acid targeted iron oxide nanoparticles. In: Bioconjugate Chemistry. 2017 ; Vol. 28, No. 1. pp. 81-87.
@article{a5230eddcb4c45f3b45b245ef4aaeb60,
title = "Folate-binding protein self-aggregation drives agglomeration of folic acid targeted iron oxide nanoparticles",
abstract = "Folate-conjugated nanomaterials have been widely investigated for drug and imaging-agent delivery. In this work, two folic acid (FA) conjugated iron oxide particles (IOP), a ∼40 nm diameter FA-IOP and a ∼450 nm diameter FA-IOP(FA-SeraMag), were synthesized. Both particles aggregated in the presence of serum folate-binding protein (FBP) at physiological concentration and buffer conditions. Mixing 0.01{\%} w/w FA-conjugated iron oxide particles with FBP-induced agglomeration generated an average hydro-dynamic particle diameter of 3800 ± 1100 nm for ∼40 nm FA-IOP and 4030 ± 1100 nm for FA-SeraMag as measured by dynamic light scattering (DLS). The presence of excess human serum albumin (HSA) (600 μM) did not prevent agglomeration of the ∼40 nm FA-IOP; however, it did inhibit agglomeration of FA-SeraMag. Atomic force microscopy measurement provided additional insight into particle morphology with the detection of individual particles in the agglomerate. This behavior is an example of a triggered cascade. A protein structural change is induced by FA binding, and the structural change favors aggregation of the ∼4 nm diameter FBPs on the particle surface; this further triggers the agglomeration of both the ∼40 and ∼450 nm diameter IOPs.",
author = "Junjie Chen and Sarah Klem and Jones, {Alexis K.} and Bradford Orr and Holl, {Mark M. Banaszak}",
doi = "10.1021/acs.bioconjchem.6b00526",
pages = "81--87",
journal = "Bioconjugate Chemistry",
Chen, J, Klem, S, Jones, AK, Orr, B & Holl, MMB 2017, 'Folate-binding protein self-aggregation drives agglomeration of folic acid targeted iron oxide nanoparticles' Bioconjugate Chemistry, vol. 28, no. 1, pp. 81-87. https://doi.org/10.1021/acs.bioconjchem.6b00526
Folate-binding protein self-aggregation drives agglomeration of folic acid targeted iron oxide nanoparticles. / Chen, Junjie; Klem, Sarah; Jones, Alexis K.; Orr, Bradford; Holl, Mark M. Banaszak.
In: Bioconjugate Chemistry, Vol. 28, No. 1, 01.01.2017, p. 81-87.
T1 - Folate-binding protein self-aggregation drives agglomeration of folic acid targeted iron oxide nanoparticles
AU - Chen, Junjie
AU - Klem, Sarah
AU - Jones, Alexis K.
AU - Orr, Bradford
AU - Holl, Mark M. Banaszak
N2 - Folate-conjugated nanomaterials have been widely investigated for drug and imaging-agent delivery. In this work, two folic acid (FA) conjugated iron oxide particles (IOP), a ∼40 nm diameter FA-IOP and a ∼450 nm diameter FA-IOP(FA-SeraMag), were synthesized. Both particles aggregated in the presence of serum folate-binding protein (FBP) at physiological concentration and buffer conditions. Mixing 0.01% w/w FA-conjugated iron oxide particles with FBP-induced agglomeration generated an average hydro-dynamic particle diameter of 3800 ± 1100 nm for ∼40 nm FA-IOP and 4030 ± 1100 nm for FA-SeraMag as measured by dynamic light scattering (DLS). The presence of excess human serum albumin (HSA) (600 μM) did not prevent agglomeration of the ∼40 nm FA-IOP; however, it did inhibit agglomeration of FA-SeraMag. Atomic force microscopy measurement provided additional insight into particle morphology with the detection of individual particles in the agglomerate. This behavior is an example of a triggered cascade. A protein structural change is induced by FA binding, and the structural change favors aggregation of the ∼4 nm diameter FBPs on the particle surface; this further triggers the agglomeration of both the ∼40 and ∼450 nm diameter IOPs.
AB - Folate-conjugated nanomaterials have been widely investigated for drug and imaging-agent delivery. In this work, two folic acid (FA) conjugated iron oxide particles (IOP), a ∼40 nm diameter FA-IOP and a ∼450 nm diameter FA-IOP(FA-SeraMag), were synthesized. Both particles aggregated in the presence of serum folate-binding protein (FBP) at physiological concentration and buffer conditions. Mixing 0.01% w/w FA-conjugated iron oxide particles with FBP-induced agglomeration generated an average hydro-dynamic particle diameter of 3800 ± 1100 nm for ∼40 nm FA-IOP and 4030 ± 1100 nm for FA-SeraMag as measured by dynamic light scattering (DLS). The presence of excess human serum albumin (HSA) (600 μM) did not prevent agglomeration of the ∼40 nm FA-IOP; however, it did inhibit agglomeration of FA-SeraMag. Atomic force microscopy measurement provided additional insight into particle morphology with the detection of individual particles in the agglomerate. This behavior is an example of a triggered cascade. A protein structural change is induced by FA binding, and the structural change favors aggregation of the ∼4 nm diameter FBPs on the particle surface; this further triggers the agglomeration of both the ∼40 and ∼450 nm diameter IOPs.
U2 - 10.1021/acs.bioconjchem.6b00526
DO - 10.1021/acs.bioconjchem.6b00526
EP - 87
JO - Bioconjugate Chemistry
JF - Bioconjugate Chemistry
Chen J, Klem S, Jones AK, Orr B, Holl MMB. Folate-binding protein self-aggregation drives agglomeration of folic acid targeted iron oxide nanoparticles. Bioconjugate Chemistry. 2017 Jan 1;28(1):81-87. https://doi.org/10.1021/acs.bioconjchem.6b00526
10.1021/acs.bioconjchem.6b00526