Nav: Home

Stereochemistry: Self-amplifying selectivity

December 05, 2016

Ludwig-Maximilians-Universitaet (LMU) in Munich chemist Oliver Trapp has designed and synthesized a catalyst which flexibly molds the handedness of the reaction products with which it interacts.

Many chemical compounds contain so-called chiral centers to which functional groups can be attached in either of two orientations. This gives rise to two different forms of the product which are mirror images of one another: Their spatial conformations are related to each other in the same way as right and left hands. Moreover, such configurational pairs - generally referred to as enantiomers - may exhibit different properties. For this reason, synthetic chemists are often faced with the problem of ensuring that the final product has the correct enantiomeric form. Oliver Trapp (Professor of Organic Chemistry at LMU since September 2016) and Golo Storch (a member of his previous research group at Heidelberg University, and currently at Yale University) now report the development of a catalyst that dynamically adapts to the stereochemistry of the compounds with which it interacts, and can progressively select for the desired enantiomer. The work is described in a paper which has just appeared in the journal Nature Chemistry.

Their system is based on a pair of molecular backbones that are known to interact with one another with enantiomeric selectivity. One of these serves as the carrier of the desired product while the other is equipped with a metal catalyst and flexible binding sites that recognize the product. The catalyst interacts transiently and repeatedly with the products of its own action, and can swiftly adjust the configuration of its binding sites. "We ourselves were surprised at how rapidly the catalyst adapts," Trapp says. These interactions effectively modify the structure of the catalyst in such a way that its stereoselectivity is enhanced. Once the catalyst has recognized the desired enantiomer, its selective efficiency improves with every further catalytic cycle. The final result of this self-amplifying action is that the end-products all have the same chiral structure.

This dynamic adaptability is of great interest in the context of the drug industry's never-ending search for biologically active compounds. Not only that, it may throw new light on how stereoselective chemical reactions operate in biological systems, where one normally finds only one chiral form of any given compound. "The world in which we live is monochiral," says Trapp. "Researchers have not yet found a convincing explanation for this. But it is conceivable that the functional principle of supermolecular interaction which we have exploited was also crucial for the origin of life."
-end-


Ludwig-Maximilians-Universität München

Related Binding Sites Articles:

Scientists uncover the structural mechanism of coronavirus receptor binding
The spike protein on the surface of the SARS-CoV-2 coronavirus can adopt at least ten distinct structural states, when in contact with the human virus receptor ACE2, according to research from the Francis Crick Institute published in Nature today (Thursday).
MAX binding with the variant Rs72780850 in RNA helicase DDX1 for susceptibility to neuroblastoma
The researchers adopted the functional polymorphism research strategy to screen out the functional polymorphisms associated with neuroblastoma in Chinese population and elucidate its mechanism, providing data on children susceptible to neuroblastoma in China.
Binding sites for protein-making machinery
ETH Zurich researchers can predict how tightly a cell's protein synthesis machinery will bind to RNA sequences - even when dealing with many billions of different RNA sequences.
Better at binding SARS-CoV-2: A variant of the human receptor for the virus as a powerful decoy
By exploring variants of a soluble version of the receptor that SARS-CoV-2 uses to binds human cells - which are being considered as therapeutic candidates that neutralize COVID-19 infection by acting as a decoy - researchers identified one that binds the virus's spike protein tightly enough to compete with spike binding by monoclonal antibodies.
Differential scanning calorimetry to quantify protein-ligand binding
A team of researchers from Kazan Federal University, Russia, led by Dr.
A new antibiotic binding site was found in the ribosome
A group of scientists from Russia, Germany and the United States, led by Skoltech scientists Ilya Osterman, Petr Sergiev, Olga Dontsova and Daniel Wilson from Hamburg University, studied the mechanism by which tetracenomycin X works, blocking the process of protein synthesis in bacteria.
Understanding differences in streptavidin-biotin binding
Beckman research scientist Rafael C. Bernardi recently published a paper that uses computational tools to explain the mechanism of how streptavidin and biotin binding is affected by streptavidin's tethering.
Cancer cells spread using a copper-binding protein
Researchers at Chalmers University of Technology, Sweden, have shown that the Atox1 protein, found in breast cancer cells, participates in the process by which cancer cells metastasise.
Using a molecular motor to switch the preference of anion-binding catalysts
Many organic molecules are chiral, which means that they are non-superimposable on their mirror image.
Self-assembling system uses magnets to mimic specific binding in DNA
A team led by Cornell University physics professors Itai Cohen and Paul McEuen is using the binding power of magnets to design self-assembling systems that potentially can be created in nanoscale form.
More Binding Sites News and Binding Sites Current Events

Trending Science News

Current Coronavirus (COVID-19) News

Top Science Podcasts

We have hand picked the top science podcasts of 2020.
Now Playing: TED Radio Hour

Listen Again: The Power Of Spaces
How do spaces shape the human experience? In what ways do our rooms, homes, and buildings give us meaning and purpose? This hour, TED speakers explore the power of the spaces we make and inhabit. Guests include architect Michael Murphy, musician David Byrne, artist Es Devlin, and architect Siamak Hariri.
Now Playing: Science for the People

#576 Science Communication in Creative Places
When you think of science communication, you might think of TED talks or museum talks or video talks, or... people giving lectures. It's a lot of people talking. But there's more to sci comm than that. This week host Bethany Brookshire talks to three people who have looked at science communication in places you might not expect it. We'll speak with Mauna Dasari, a graduate student at Notre Dame, about making mammals into a March Madness match. We'll talk with Sarah Garner, director of the Pathologists Assistant Program at Tulane University School of Medicine, who takes pathology instruction out of...
Now Playing: Radiolab

Kittens Kick The Giggly Blue Robot All Summer
With the recent passing of Ruth Bader Ginsburg, there's been a lot of debate about how much power the Supreme Court should really have. We think of the Supreme Court justices as all-powerful beings, issuing momentous rulings from on high. But they haven't always been so, you know, supreme. On this episode, we go all the way back to the case that, in a lot of ways, started it all.  Support Radiolab by becoming a member today at Radiolab.org/donate.