Facile production of multivalent enzyme-nanoparticle conjugates

Sam J. Kuhn; Stephanie K. Finch; Dennis E. Hallahan; Todd D. Giorgio

doi:10.1016/j.jmmm.2006.10.1165

Facile production of multivalent enzyme-nanoparticle conjugates

Sam J. Kuhn, Stephanie K. Finch, Dennis E. Hallahan, Todd D. Giorgio

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

Nanoparticles (NPs) enable the development of new, biologically relevant, multifunctional agents. Multifunctional NPs can mimic the invasive biological processes involved in cancer metastasis. We have demonstrated a facile and controllable method of conjugating multiple enzyme species to superparamagnetic (SPM) NPs. Horseradish peroxidase, α-glucosidase, and collagenase were conjugated to SPM NPs with a functional enzyme:NP ratio of 15:127:103:1. N-succinimidyl-S-acetylthiopropionate (SATP)-mediated addition of sulfhydryls to enzymes was achieved without significant activity loss. Conjugation of all enzymes was simultaneously accomplished using maleimide reactive groups generated from activation of amines associated with polyethylene glycol molecules on the NP surface. Cross reactivity between enzyme activity assay systems was negligible.

Original language	English
Pages (from-to)	68-72
Number of pages	5
Journal	Journal of Magnetism and Magnetic Materials
Volume	311
Issue number	1 SPEC. ISS.
DOIs	https://doi.org/10.1016/j.jmmm.2006.10.1165
State	Published - Apr 2007

Keywords

Conjugation
Enzyme
Multifunctional
Nanoparticle
Superparamagnetic

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10.1016/j.jmmm.2006.10.1165

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title = "Facile production of multivalent enzyme-nanoparticle conjugates",

abstract = "Nanoparticles (NPs) enable the development of new, biologically relevant, multifunctional agents. Multifunctional NPs can mimic the invasive biological processes involved in cancer metastasis. We have demonstrated a facile and controllable method of conjugating multiple enzyme species to superparamagnetic (SPM) NPs. Horseradish peroxidase, α-glucosidase, and collagenase were conjugated to SPM NPs with a functional enzyme:NP ratio of 15:127:103:1. N-succinimidyl-S-acetylthiopropionate (SATP)-mediated addition of sulfhydryls to enzymes was achieved without significant activity loss. Conjugation of all enzymes was simultaneously accomplished using maleimide reactive groups generated from activation of amines associated with polyethylene glycol molecules on the NP surface. Cross reactivity between enzyme activity assay systems was negligible.",

keywords = "Conjugation, Enzyme, Multifunctional, Nanoparticle, Superparamagnetic",

author = "Kuhn, {Sam J.} and Finch, {Stephanie K.} and Hallahan, {Dennis E.} and Giorgio, {Todd D.}",

note = "Funding Information: This work was supported by the US Army Medical Research and Materiel Command BCRP-CDMRP: BC023387.",

year = "2007",

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doi = "10.1016/j.jmmm.2006.10.1165",

language = "English",

volume = "311",

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journal = "Journal of Magnetism and Magnetic Materials",

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TY - JOUR

T1 - Facile production of multivalent enzyme-nanoparticle conjugates

AU - Kuhn, Sam J.

AU - Finch, Stephanie K.

AU - Hallahan, Dennis E.

AU - Giorgio, Todd D.

N1 - Funding Information: This work was supported by the US Army Medical Research and Materiel Command BCRP-CDMRP: BC023387.

PY - 2007/4

Y1 - 2007/4

N2 - Nanoparticles (NPs) enable the development of new, biologically relevant, multifunctional agents. Multifunctional NPs can mimic the invasive biological processes involved in cancer metastasis. We have demonstrated a facile and controllable method of conjugating multiple enzyme species to superparamagnetic (SPM) NPs. Horseradish peroxidase, α-glucosidase, and collagenase were conjugated to SPM NPs with a functional enzyme:NP ratio of 15:127:103:1. N-succinimidyl-S-acetylthiopropionate (SATP)-mediated addition of sulfhydryls to enzymes was achieved without significant activity loss. Conjugation of all enzymes was simultaneously accomplished using maleimide reactive groups generated from activation of amines associated with polyethylene glycol molecules on the NP surface. Cross reactivity between enzyme activity assay systems was negligible.

AB - Nanoparticles (NPs) enable the development of new, biologically relevant, multifunctional agents. Multifunctional NPs can mimic the invasive biological processes involved in cancer metastasis. We have demonstrated a facile and controllable method of conjugating multiple enzyme species to superparamagnetic (SPM) NPs. Horseradish peroxidase, α-glucosidase, and collagenase were conjugated to SPM NPs with a functional enzyme:NP ratio of 15:127:103:1. N-succinimidyl-S-acetylthiopropionate (SATP)-mediated addition of sulfhydryls to enzymes was achieved without significant activity loss. Conjugation of all enzymes was simultaneously accomplished using maleimide reactive groups generated from activation of amines associated with polyethylene glycol molecules on the NP surface. Cross reactivity between enzyme activity assay systems was negligible.

KW - Conjugation

KW - Enzyme

KW - Multifunctional

KW - Nanoparticle

KW - Superparamagnetic

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U2 - 10.1016/j.jmmm.2006.10.1165

DO - 10.1016/j.jmmm.2006.10.1165

M3 - Article

AN - SCOPUS:33947154737

SN - 0304-8853

VL - 311

SP - 68

EP - 72

JO - Journal of Magnetism and Magnetic Materials

JF - Journal of Magnetism and Magnetic Materials

IS - 1 SPEC. ISS.

ER -

Facile production of multivalent enzyme-nanoparticle conjugates

Abstract

Keywords

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