Purification of protein therapeutics via high-affinity supramolecular host-guest interactions.

Efficient purification is crucial to providing large quantities of recombinant therapeutic proteins, such as monoclonal antibodies and cytokines. However, affinity techniques for manufacturing protein therapeutics that use biomolecule-conjugated agarose beads that harness specific biomolecular interactions suffer from issues related to protein denaturation, contamination and the need to maintain biomolecule-specific conditions for efficient protein capture. Here, we report a versatile and scalable method for the purification of recombinant protein therapeutics.

Supra-blot: an accurate and reliable assay for detecting target proteins with a synthetic host molecule-enzyme hybrid.

In accordance with the rapid increase in demand for selective and spatial chemical tagging, and accurate detection of proteins of interest, we develop a sensitive protein detection method, termed "Supra-blot" capitalizing on high-affinity host-guest interaction between cucurbit[7]uril (CB[7]) and adamantylammonium (AdA). The method can directly detect chemically tagged proteins without false-positive signals caused by endogenous biomolecules. Not only a single specific protein, but also spatially localized proteins in cells were labeled with AdA, and selectively detected by a host molecule-enzyme hybrid, CB[7]-conjugated horseradish peroxidase (CB[7]-HRP) generating amplified chemiluminescence signals.

Superacid-Mediated Functionalization of Hydroxylated Cucurbit[]urils.

Herein we report a facile transformation of hydroxylated cucurbit[]uril (CB[], = 6 and 7) to other functionality-conjugated CB[]s by nucleophilic substitution of the hydroxyl group with a wide range of nitriles and alcohols. The reaction proceeds efficiently via generation of a superelectrophilic carbocation on the CB framework from hydroxylated CB[]s under superacidic conditions. One of the resulting CB[] derivatives with reactive functionality, monocarboxylated CB[7], is efficiently conjugated to an enzyme (horseradish peroxidase, HRP) by amide coupling.

Self-assembled adhesive biomaterials formed by a genetically designed fusion protein.

Here we report a recombinant protein (MS) obtained by genetic fusion of a mussel foot protein (Mfp3) motif into a silk spidroin (MaSp1). The MS not only self-assembled into a supramolecular fibre, as does the parent MaSp1, but also showed enhanced adhesiveness resulting from the DOPA-containing Mfp3 portion. The successful incorporation of the wet adhesiveness of Mfp3 into the well-structured assembly of MaSp1 may provide a new insight for the genetic design of underwater adhesive recombinant proteins by utilizing the structural features of a spidroin protein.

High-power lithium-ion capacitor using LiMnBO3 -nanobead anode and polyaniline-nanofiber cathode with excellent cycle life.

LiMnBO3 nanobeads (LMB-NB) with uniform size and distribution were synthesized using a urea-assisted microwave/solvothermal method. The potential application of LMB-NBs as an anode for a lithium-ion hybrid capacitor (Li-AHC) was tested with a polyaniline-nanofiber (PANI-NF) cathode in a nonaqueous LiPF6 (1 M)-ethylene carbonate/dimethyl carbonate electrolyte. Cyclic voltammetry (CV) and charge-discharge (C/DC) studies revealed that the PANI-NF/LMB-NB cell showed an exceptional capacitance behavior between 0-3 V along with a prolonged cycle life.