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An inorganic sandwich molecule, Na[Co(C2B9H11)2], able to produce vesicles through self-assembling, and known to produce strong dihydrogen bond interactions with amine groups shall be capable of interacting with proteins. This dual non-bonding ability of Na[Co(C2B9H11)2], is what makes this molecule unique both to be firmly anchored and capable of extending on a protein surface. To prove so, the widely available Bovine Serum Albumin that has many pendant amino groups in its structure has been taken as the model protein. It is found that around 100 molecules of Na[Co(C2B9H11)2], preserve the native structure of BSA, while endorsing it with a significantly increased stability in front of chemical and thermal induced denaturation due to an efficient encapsulation. The advantages of this encapsulation technique are two, one is its simplicity as it relies in the anchoring capacity of Na[Co(C2B9H11)2] to the surface of the protein through the amine containing residues and two, its self-assembling capacity allowing to spread on the surface. The dense protection shield by the Na[Co(C2B9H11)2] has been demonstrated by the inhibition of BSA pseudo-esterase activity which indicates that the inorganic corset around BSA protects its superficial reactive residues, preventing their acetylation.
This article was published in the following journal.
Name: Chemistry (Weinheim an der Bergstrasse, Germany)
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