Entrapment of integral membrane proteins (IMPs) in transparent, nanoporous silica gels has proven to be a challenge, as current and previous techniques utilize liposomes as biological membrane hosts. The instability of liposomes in nanoporous gels is attributed to their size (~100 nm) and altered structure and lipid dynamics upon entrapment within the nanometer scale pores (5-50 nm) of silica gel. This ultimately results in disruption of protein activity. We intend to overcome these barriers by using nanolipoprotein particles (NLPs) as biomembrane hosts. NLPs are discoidal patches of lipid bilayer that are belted by amphiphilic scaffold proteins and have an average thickness of 5 nm, with diameters ranging from 10-15 nm. The IMP-NLP complexes are synthesized in a cell-free environment, which circumvents traditional protein reconstitution in membranes.  Bacteriorhodopsin - a robust IMP that indicates its proper conformation via distinct purple coloration – will serve as a model IMP for this system.   To ensure proper functioning of the system, we have investigated the phase behavior of the lipids and the secondary structure and environmental polarity of the scaffold proteins in gel-entrapped NLPs.  In addition, we will present preliminary data on the physical and spectral properties of entrapped and non-entrapped bacteriorhodopsin-NLPs. <br/>

Nanolipoprotein particles entrapped within nanoporous silica gel

249th National Meeting (2015)

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