Sikder, Amrita; Ray, Debes; Aswal, Vinod K.; Ghosh, Suhrit published the artcile< Supramolecular Assembly of a Molecularly Engineered Protein and Polymer>, Computed Properties of 2127-03-9, the main research area is supramol assembly protein polymer; conjugation; hydrogen bonds; polymers; proteins; self-assembly.
Programmable assembly of biomols. is a fast growing research area that aims to emulate nature’s elegance in creating numerous hierarchical self-assembled structures, which are responsible for unimaginably difficult biol. functions. Protein assembly is a particularly challenging task, owing to their structural diversity, conformational heterogeneity, and high mol. weight This article reveals the ability of a supramol. structure-directing unit (SSDU) to regulate the entropically favorable supramol. assembly of a covalently conjugated protein (bovine serum albumin (BSA)) to produce well-defined protein-decorated micelles with remarkably high thermal stability, suppression of the thermal denaturation of the protein, and retention of enzymic activity. Furthermore, a SSDU-appended thermo-responsive poly(N-isopropylacrylamide) (PNIPAM) coassembles with the SSDU-BSA conjugate because, in both cases, assembly was primarily driven by specific mol. recognition between the SSDUs. However, the resulting supramol. protein-polymer conjugate exhibits distinctly different polymersome structure to that of the micellar particle produced by the protein-SSDU conjugate. In this case, the enzymic activity can be significantly suppressed above the lower critical solution temperature of supramolecularly conjugated PNIPAM, possibly due to collapse of the de-solvated polymer chains on the protein surface.
Chemistry – A European Journal published new progress about Bovine serum albumin Role: PEP (Physical, Engineering or Chemical Process), PRP (Properties), PROC (Process) (conjugates with 1,4,5,8-naphthalenetetracarboxylic diimide derivative). 2127-03-9 belongs to class pyridine-derivatives, and the molecular formula is C10H8N2S2, Computed Properties of 2127-03-9.