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dc.contributor.authorLlauro, Aida
dc.contributor.authorGuerra, Pablo
dc.contributor.authorKant, Ravi
dc.contributor.authorBothner, Brian
dc.contributor.authorVerdaguer, Nuria
dc.contributor.authorde Pablo, Pedro J
dc.identifier.citationLlauro, Aida , Pablo Guerra, Ravi Kant, Brian Bothner, Nuria Verdaguer, and Pedro J de Pablo. "Decrease in pH destabilizes individual vault nanocages by weakening the inter-protein lateral interaction." Scientific Reports 6 (October 2016): 34143. DOI:
dc.description.abstractVault particles are naturally occurring proteinaceous cages with promising application as molecular containers. The use of vaults as functional transporters requires a profound understanding of their structural stability to guarantee the protection and controlled payload delivery. Previous results performed with bulk techniques or at non-physiological conditions have suggested pH as a parameter to control vault dynamics. Here we use Atomic Force Microscopy (AFM) to monitor the structural evolution of individual vault particles while changing the pH in real time. Our experiments show that decreasing the pH of the solution destabilize the barrel region, the central part of vault particles, and leads to the aggregation of the cages. Additional analyses using Quartz-Crystal Microbalance (QCM) and Differential Scanning Fluorimetry (DSF) are consistent with our single molecule AFM experiments. The observed topographical defects suggest that low pH weakens the bonds between adjacent proteins. We hypothesize that the observed effects are related to the strong polar character of the protein-protein lateral interactions. Overall, our study unveils the mechanism for the influence of a biologically relevant range of pHs on the stability and dynamics of vault particles.en_US
dc.description.sponsorshipSpanish Ministry of Economy and Competitiveness; Spanish Excellence Network of Physical Virology; National Institutes of Healthen_US
dc.titleDecrease in pH destabilizes individual vault nanocages by weakening the inter-protein lateral interactionen_US
mus.citation.journaltitleScientific Reportsen_US
mus.identifier.categoryChemical & Material Sciencesen_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentChemistry & Biochemistry.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.contributor.orcidBothner, Brian|0000-0003-1295-9609en_US

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