80280-49-5Relevant academic research and scientific papers
Rational Design of Supramolecular Dynamic Protein Assemblies by Using a Micelle-Assisted Activity-Based Protein-Labeling Technology
Sandanaraj, Britto S.,Reddy, Mullapudi Mohan,Bhandari, Pavankumar Janardhan,Kumar, Sugam,Aswal, Vinod K.
, p. 16085 - 16096 (2018/10/15)
The self-assembly of proteins into higher-order superstructures is ubiquitous in biological systems. Genetic methods comprising both computational and rational design strategies are emerging as powerful methods for the design of synthetic protein complexes with high accuracy and fidelity. Although useful, most of the reported protein complexes lack a dynamic behavior, which may limit their potential applications. On the contrary, protein engineering by using chemical strategies offers excellent possibilities for the design of protein complexes with stimuli-responsive functions and adaptive behavior. However, designs based on chemical strategies are not accurate and therefore, yield polydisperse samples that are difficult to characterize. Here, we describe simple design principles for the construction of protein complexes through a supramolecular chemical strategy. A micelle-assisted activity-based protein-labeling technology has been developed to synthesize libraries of facially amphiphilic synthetic proteins, which self-assemble to form protein complexes through hydrophobic interaction. The proposed methodology is amenable for the synthesis of protein complex libraries with molecular weights and dimensions comparable to naturally occurring protein cages. The designed protein complexes display a rich structural diversity, oligomeric states, sizes, and surface charges that can be engineered through the macromolecular design. The broad utility of this method is demonstrated by the design of most sophisticated stimuli-responsive systems that can be programmed to assemble/disassemble in a reversible/irreversible fashion by using the pH or light as trigger.
Carbohydrate-protein interactions at interfaces: Comparison of the binding of Ricinus communis lectin to two series of synthetic glycolipids using surface plasmon resonance studies
Critchley,Clarkson
, p. 4148 - 4159 (2007/10/03)
Two C-lactosyl lipids and the related C-galactosyl lipids have been synthesised and their binding to RCA120 plant lectin was compared with a second series of thiolactosylethoxyalkanes. The interactions were measured quantitatively in real time by surface plasmon resonance (BIAcore) at a range of concentrations and temperatures from 5 to 30°C. The C-galactosyl lipid (1,3-dimethyl-5-[β-D-galactopyranosyl]-5-(4-octadecyloxybenzyl)pyrimidine-2 ,4,6-trione) bound much more weakly with a KA = 8.86 × 105 than the corresponding C-lactosyl lipid (1,3-dimethyl-5-[β-D-galactopyranosyl-(1 → 4)-β-D-glucopyranosyl]-5-(4-octadecyloxybenzyl)pyrimidine-2,4,6-trione) (KA = 2.31 × 107). The influence of the linker region of the two different series of lactosyl lipids was clearly demonstrated by the differences in the binding to RCA120 lectin. The changes in kinetic values and in the enthalpic and entropic contribution to the free energy of binding reflected the importance of the linker and the hydrocarbon anchor holding the synthetic glycolipids in the neomembrane.
Smectic Bimetallomesogens: Synthesis and Mesomorphic Properties in Oxygen-Bridged Dicopper and Divanadyl Complexes
Leu, Yi-Fun,Lai, Chung K.
, p. 89 - 91 (2007/10/03)
The synthesis and mesomorphic properties of a homologous series of N-(3-hydroxypropyl)-4-alkoxylsalicylaldimine, N-(3-hydroxypropyl)-4-(4′-alkoxybenzoxy)salicylaldimine, and their dicopper(II) and dioxovanadium(VI) complexes are reported. Copper complexes
