Conserved Activity of Reassociated Homotetrameric Protein Subunits Released from Mesoporous Silica Nanoparticles.
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.
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