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000856725 1001_ $$0P:(DE-HGF)0$$aSiefker, Justin$$b0
000856725 245__ $$aConfinement Facilitated Protein Stabilization As Investigated by Small-Angle Neutron Scattering
000856725 260__ $$aWashington, DC$$bAmerican Chemical Society$$c2018
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000856725 520__ $$aWhile 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.
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000856725 7001_ $$0P:(DE-Juel1)130542$$aBiehl, Ralf$$b1
000856725 7001_ $$0P:(DE-Juel1)130777$$aKruteva, Margarita$$b2$$eCorresponding author
000856725 7001_ $$0P:(DE-Juel1)144382$$aFeoktystov, Artem$$b3$$ufzj
000856725 7001_ $$00000-0002-1810-2537$$aCoppens, Marc-Olivier$$b4$$eCorresponding author
000856725 773__ $$0PERI:(DE-600)1472210-0$$a10.1021/jacs.8b08454$$gVol. 140, no. 40, p. 12720 - 12723$$n40$$p12720 - 12723$$tJournal of the American Chemical Society$$v140$$x1520-5126$$y2018
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