The unique self-assembly/disassembly property of Archaeoglobus fulgidus ferritin and its implications on molecular release from the protein cage

Biochimica Et Biophysica Acta
Barindra SanaSierin Lim

Abstract

In conventional in vitro encapsulation of molecular cargo, the multi-subunit ferritin protein cages are disassembled in extremely acidic pH and re-assembled in the presence of highly concentrated cargo materials, which results in poor yields due to the low-pH treatment. In contrast, Archaeoglobus fulgidus open-pore ferritin (AfFtn) and its closed-pore mutant (AfFtn-AA) are present as dimeric species in neutral buffers that self-assemble into cage-like structure upon addition of metal ions. To understand the iron-mediated self-assembly and ascorbate-mediated disassembly properties, we studied the iron binding and release profile of the AfFtn and AfFtn-AA, and the corresponding oligomerization of their subunits. Fe(2+) binding and conversion to Fe(3+) triggered the self-assembly of cage-like structures from dimeric species of AfFtn and AfFtn-AA subunits, while disassembly was induced by dissolving the iron core with reducing agents. The closed-pore AfFtn-AA has identical iron binding kinetics but lower iron release rates when compared to AfFtn. While the iron binding rate is proportional to Fe(2+) concentration, the iron release rate can be controlled by varying ascorbate concentrations. The AfFtn and AfFtn-AA cages formed by iro...Continue Reading

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Citations

Dec 13, 2016·Nanoscale·Valeria de TurrisPaola Baiocco
Jul 26, 2018·Genes·Dennis DiazAnwar Sunna
Jun 21, 2020·Nature Communications·Luis E Contreras-LlanoCheemeng Tan
Feb 16, 2021·Chemical Society Reviews·Chenyan LvGuanghua Zhao
Dec 1, 2020·Journal of the American Chemical Society·Kristian Le VayAdam W Perriman
Jul 2, 2021·Nanoscale·Mantu KumarJonathan G Heddle
Sep 4, 2021·Materials Science & Engineering. C, Materials for Biological Applications·Ambrish KumarSierin Lim

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