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Conserved Activity of Reassociated Homotetrameric Protein Subunits Released from Mesoporous Silica Nanoparticles.
Deodhar, Gauri V; Adams, Marisa L; Joardar, Sutapa; Joglekar, Madhura; Davidson, Malcolm; Smith, William C; Mettler, Madelyn; Toler, Sydney A; Davies, Fiona K; Williams, S Kim R; Trewyn, Brian G.
Affiliation
  • Deodhar GV; Department of Chemistry, Colorado School of Mines , Golden, Colorado 80401, United States.
  • Adams ML; Department of Chemistry, Colorado School of Mines , Golden, Colorado 80401, United States.
  • Joardar S; Department of Chemistry, Colorado School of Mines , Golden, Colorado 80401, United States.
  • Joglekar M; Department of Chemistry, Colorado School of Mines , Golden, Colorado 80401, United States.
  • Davidson M; Department of Chemistry, Colorado School of Mines , Golden, Colorado 80401, United States.
  • Smith WC; Department of Chemistry, Colorado School of Mines , Golden, Colorado 80401, United States.
  • Mettler M; Department of Chemistry, Colorado School of Mines , Golden, Colorado 80401, United States.
  • Toler SA; Department of Chemistry, Colorado School of Mines , Golden, Colorado 80401, United States.
  • Davies FK; Department of Chemistry, Colorado School of Mines , Golden, Colorado 80401, United States.
  • Williams SKR; Department of Chemistry, Colorado School of Mines , Golden, Colorado 80401, United States.
  • Trewyn BG; Department of Chemistry, Colorado School of Mines , Golden, Colorado 80401, United States.
Langmuir ; 34(1): 228-233, 2018 01 09.
Article in En | MEDLINE | ID: mdl-29231740
ABSTRACT
Mesoporous silica nanoparticles (MSN) with enlarged pores were prepared and characterized, and reversibly dissociated subunits of concanavalin A were entrapped in the mesopores, as shown by multiple biochemical and material characterizations. When loaded in the MSN, we demonstrated protein stability from proteases and, upon release, the subunits reassociated into active proteins shown through mannose binding and o-phthalaldehyde fluorescence. We have demonstrated a versatile and facile method to load homomeric proteins into MSN with potential applications in enhancing the delivery of large therapeutic proteins.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Drug Carriers / Silicon Dioxide / Concanavalin A / Protein Subunits / Nanoparticles / Protein Multimerization Language: En Journal: Langmuir Journal subject: QUIMICA Year: 2018 Document type: Article Affiliation country: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Drug Carriers / Silicon Dioxide / Concanavalin A / Protein Subunits / Nanoparticles / Protein Multimerization Language: En Journal: Langmuir Journal subject: QUIMICA Year: 2018 Document type: Article Affiliation country: United States