Simple Synthetic Lectin Binds Glucose | Chemical & Engineering News
Volume 90 Issue 32 | p. 35 | Concentrates
Issue Date: August 6, 2012

Simple Synthetic Lectin Binds Glucose

Easy-to-make synthetic receptor has sugar recognition properties similar to more-complicated previous versions
Department: Science & Technology
News Channels: Biological SCENE
Keywords: lectin, carbohydrate, glucose, sugars, sensor

Carbohydrate recognition in aqueous solutions is difficult, even for the carbohydrate-binding proteins known as lectins, because the hydroxyl-rich carbohydrates blend in with the water background. Synthetic molecules that mimic those proteins have tended to be complicated and hard to make. Now, Anthony P. Davis and coworkers at the University of Bristol, in England, report a synthetic water-soluble macro­cyclic lectin that they can synthesize in five steps at 23% overall yield, compared with 20 steps and 0.1% overall yield for an earlier version (Nat. Chem., DOI: 10.1038/nchem.1409). The new lectin has a simpler structure than the earlier one but similar recognition properties. It is selective for glucose relative to other common monosaccharides, with an affinity for glucose 50 times that for galactose. In addition, because it includes anthracene units, the new lectin has a built-in fluorescence-signaling mechanism. The molecule’s fluorescence intensity changes in response to the addition of glucose. The lectin is sensitive to glucose at concentrations relevant for blood glucose monitoring.

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Khushi Matta (July 17, 2013 5:13 PM)
Is it commercially available? is it cheaper than other glucose binding lectins ?

because i am looking for use of such lectin for other innovative and robust discoveries

and I need at affordable price
Tom Carter (January 23, 2015 6:59 AM)
This is not currently commercially available but Ziylo Ltd are currently looking at demand, contact if you're still interested.

Tom Carter (January 23, 2015 7:01 AM)
We have just published the next generation of this sensor, it shows 50% stronger binding with a much bigger change in fluorescence on binding. Interestingly this has been facilitated by adjusting the dendrimeric groups. Check it out here:

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