Chakraborty, Saptarshi; Khamrui, Rajesh; Ghosh, Suhrit published the artcile< Redox responsive activity regulation in exceptionally stable supramolecular assembly and co-assembly of a protein>, Recommanded Product: 1,2-Di(pyridin-2-yl)disulfane, the main research area is protein supramol assembly redox responsive activity.
Supramol. assembly of biomols./macromols. stems from the desire to mimic complex biol. structures and functions of living organisms. While DNA nanotechnol. is already in an advanced stage, protein assembly is still in its infancy as it is a significantly difficult task due to their large mol. weight, conformational complexity and structural instability towards variation in temperature, pH or ionic strength. This article reports highly stable redox-responsive supramol. assembly of a protein Bovine serum albumin (BSA) which is functionalized with a supramol. structure directing unit (SSDU). The SSDU consists of a benzamide functionalized naphthalene-diimide (NDI) chromophore which is attached with the protein by a bio-reducible disulfide linker. The SSDU attached protein (NDI-BSA) exhibits spontaneous supramol. assembly in water by off-set π-stacking among the NDI chromophores, leading to the formation of spherical nanoparticles (diameter: 150-200 nm). The same SSDU when connected with a small hydrophilic wedge (NDI-1) instead of the large globular protein, exhibits a different π-stacking mode with relatively less longitudinal displacement which results in a fibrillar network and hydrogelation. Supramol. co-assembly of NDI-BSA and NDI-1 (3 : 7) produces similar π-stacking and an entangled 1D morphol. Both the spherical assembly of NDI-BSA or the fibrillar co-assembly of NDI-BSA + NDI-1 (3 : 7) provide sufficient thermal stability to the protein as its thermal denaturation could be completely surpassed while the secondary structure remained intact. However, the esterase like activity of the protein reduced significantly as a result of such supramol. assembly indicating limited access by the substrate to the active site of the enzyme located in the confined environment. In the presence of glutathione (GSH), a biol. important tri-peptide, due to the cleavage of the disulfide bond, the protein became free and was released, resulting in fully regaining its enzymic activity. Such supramol. assembly provided excellent protection to the protein against enzymic hydrolysis as the relative hydrolysis was estimated to be <30% for the co-assembled protein with respect to the free protein under identical conditions. Similar to bioactivity, the enzymic hydrolysis also became prominent after GSH-treatment, confirming that the lack of hydrolysis in the supramolecularly assembled state is indeed related to the confinement of the protein in the nanostructure assembly. Chemical Science published new progress about Absorption. 2127-03-9 belongs to class pyridine-derivatives, and the molecular formula is C10H8N2S2, Recommanded Product: 1,2-Di(pyridin-2-yl)disulfane.