938190-77-3Relevant academic research and scientific papers
A semisynthetic fluorescent sensor protein for glutamate
Brun, Matthias A.,Tan, Kui-Thong,Griss, Rudolf,Kielkowska, Anna,Reymond, Luc,Johnsson, Kai
, p. 7676 - 7678 (2012)
We report the semisynthesis of a fluorescent glutamate sensor protein on cell surfaces. Sensor excitation at 547 nm yields a glutamate-dependent emission spectrum between 550 and 700 nm that can be exploited for ratiometric sensing. On cells, the sensor displays a ratiometric change of 1.56. The high sensitivity toward glutamate concentration changes of the sensor and its exclusive extracellular localization make it an attractive tool for glutamate sensing in neurobiology.
Stapling of two PEGylated side chains increases the conformational stability of the WW domain via an entropic effect
Xiao, Qiang,Bécar, Natalie A.,Brown, Nathaniel P.,Smith, Mason S.,Stern, Kimberlee L.,Draper, Steven R.E.,Thompson, Katherine P.,Price, Joshua L.
supporting information, p. 8933 - 8939 (2018/12/10)
Hydrocarbon stapling and PEGylation are distinct strategies for enhancing the conformational stability and/or pharmacokinetic properties of peptide and protein drugs. Here we combine these approaches by incorporating asparagine-linked O-allyl PEG oligomers at two positions within the β-sheet protein WW, followed by stapling of the PEGs via olefin metathesis. The impact of stapling two sites that are close in primary sequence is small relative to the impact of PEGylation alone and depends strongly on PEG length. In contrast, stapling of two PEGs that are far apart in primary sequence but close in tertiary structure provides substantially more stabilization, derived mostly from an entropic effect. Comparison of PEGylation + stapling vs. alkylation + stapling at the same positions in WW reveals that both approaches provide similar overall levels of conformational stability.
