Sweeter and stronger: enhancing sweetness and stability of the single chain monellin MNEI through molecular design
Citations Over TimeTop 10% of 2016 papers
Abstract
Sweet proteins are a family of proteins with no structure or sequence homology, able to elicit a sweet sensation in humans through their interaction with the dimeric T1R2-T1R3 sweet receptor. In particular, monellin and its single chain derivative (MNEI) are among the sweetest proteins known to men. Starting from a careful analysis of the surface electrostatic potentials, we have designed new mutants of MNEI with enhanced sweetness. Then, we have included in the most promising variant the stabilising mutation E23Q, obtaining a construct with enhanced performances, which combines extreme sweetness to high, pH-independent, thermal stability. The resulting mutant, with a sweetness threshold of only 0.28 mg/L (25 nM) is the strongest sweetener known to date. All the new proteins have been produced and purified and the structures of the most powerful mutants have been solved by X-ray crystallography. Docking studies have then confirmed the rationale of their interaction with the human sweet receptor, hinting at a previously unpredicted role of plasticity in said interaction.
Related Papers
- → Improved single-chain-magnet behavior in a biradical-based nitronyl nitroxide-Cu–Dy chain(2019)48 cited
- → Freely jointed chain models with extensible links(2022)24 cited
- → Two Trihydrazine‐Bridged Cobalt(II) Chain Compounds Exhibiting Antiferromagnetic Ordering and Single‐Chain Magnetic Behavior(2014)9 cited
- → Molecular Motion of an Isolated Single Chain Cellulose Molecule(2004)2 cited
- Single-chain Condensed State and Interpenetrated Multi-chain Condensed State of Polymers(2000)