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Protein-templated gold nanoparticle synthesis: protein organization, controlled gold sequestration, and unexpected reaction products.
Hart, Cassidy; Abuladel, Nouf; Bee, Madeleine; Kreider, Megan C; CVitan, Alexander C; Esson, Moira M; Farag, Andrew; Ibeh, Trisha; Kalivas, Eleni N; Larco, Daniel-Mario; Walker Long, Andrew; Lymperopoulos, Loukas; Mendel, Zachary; Miles, Nancy; Zareba, Carly M; Schwabacher, James C; Slucher, Helen; Vinals, Javier; Heddleston, John M; Li, Wenyue; Fox, Douglas M; Hartings, Matthew R.
Afiliación
  • Hart C; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Abuladel N; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Bee M; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Kreider MC; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • CVitan AC; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Esson MM; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Farag A; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Ibeh T; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Kalivas EN; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Larco DM; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Walker Long A; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Lymperopoulos L; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Mendel Z; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Miles N; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Zareba CM; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Schwabacher JC; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Slucher H; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Vinals J; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Heddleston JM; Semiconductor and Dimensional Metrology Division, National Institute of Standards and Technology, Gaithersburg, MD 20899, USA.
  • Li W; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Fox DM; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
  • Hartings MR; Department of Chemistry, American University, 4400 Massachusetts Ave, NW, Washington, DC 20016, USA. hartings@american.edu.
Dalton Trans ; 46(47): 16465-16473, 2017 Dec 21.
Article en En | MEDLINE | ID: mdl-29144523
Emerging applications that exploit the properties of nanoparticles for biotechnology require that the nanoparticles be biocompatible or support biological recognition. These types of particles can be produced through syntheses that involve biologically relevant molecules (proteins or natural extracts, for example). Many of the protocols that rely on these molecules are performed without a clear understanding of the mechanism by which the materials are produced. We have investigated a previously described reaction in which gold nanoparticles are produced from the reaction of chloroauric acid and proteins in solution. We find that modifications to the starting conditions can alter the product from the expected solution-suspended colloids to a product where colloids are formed within a solid, fibrous protein structure. We have interrogated this synthesis, exploiting the change in products to better understand this reaction. We have evaluated the kinetics and products for 7 different proteins over a range of concentrations and temperatures. The key factor that controls the synthetic outcome (colloid or fiber) is the concentration of the protein relative to the gold concentration. We find that the observed fibrous structures are more likely to form at low protein concentrations and when hydrophilic proteins are used. An analysis of the reaction kinetics shows that AuNP formation occurs faster at lower protein (fiber-forming) concentrations than at higher protein (colloid-forming) concentrations. These results contradict traditional expectations for reaction kinetics and protein-fiber formation and are instructive of the manner in which proteins template gold nanoparticle production.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas / Nanotecnología / Nanopartículas del Metal / Oro Límite: Animals Idioma: En Revista: Dalton Trans Asunto de la revista: QUIMICA Año: 2017 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas / Nanotecnología / Nanopartículas del Metal / Oro Límite: Animals Idioma: En Revista: Dalton Trans Asunto de la revista: QUIMICA Año: 2017 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido