Journal Article FZJ-2018-06076

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Confinement Facilitated Protein Stabilization As Investigated by Small-Angle Neutron Scattering

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2018
American Chemical Society Washington, DC

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Abstract: While mesoporous silicas have been shown to bea compelling candidate for drug delivery and the implemen-tation of biotechnological applications requiring protein con-finement and immobilization, the understanding of protein be-haviour upon physical adsorption into silica pores is limited.Many indirect methods are available to assess general adsorbedproteinstability, suchasFTIRandactivityassays. However, thelimitation of these methods is that spatial protein arrangementwithin the pores cannot be assessed. Mesoporous silicas pose adistinct challenge to direct methods, such as TEM, which lacksthe contrast and resolution required to adequately observe im-mobilized protein structure, and NMR, which is computation-ally intensive and requires knowledge of the primary structurea priori. Small-angle neutron scattering (SANS) can surmountthese limitations and observe spatial protein arrangement withinpores. Hereby, we observe the stabilization of fluid-like proteinarrangement, facilitated by geometry-dependent crowding ef-fects in cylindrical pores of ordered mesoporous silica, SBA-15.Stabilization is induced from a fluid-like structure factor, whichis observed for samples at maximum protein loading in SBA-15with pore diameters of 6.4 and 8.1 nm. Application of thiseffect for prevention of irreversible aggregation in high concen-tration environments is proposed.

Keyword(s): Polymers, Soft Nano Particles and Proteins (1st) ; Biology (2nd)

Classification:

Contributing Institute(s):
  1. JCNS-FRM-II (JCNS-FRM-II)
  2. Neutronenstreuung (Neutronenstreuung ; JCNS-1)
Research Program(s):
  1. 6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623) (POF3-623)
  2. 6G15 - FRM II / MLZ (POF3-6G15) (POF3-6G15)
Experiment(s):
  1. KWS-1: Small angle scattering diffractometer (NL3b)

Appears in the scientific report 2018
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Medline ; Creative Commons Attribution CC BY 4.0 ; OpenAccess ; BIOSIS Previews ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; IF >= 10 ; JCR ; NCBI Molecular Biology Database ; NationallizenzNationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection
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Institute Collections > JCNS > JCNS-FRM-II
Document types > Articles > Journal Article
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 Record created 2018-10-26, last modified 2021-01-29