Like Koeng laid, artificial enzymes are very inefficient atm. If you make them from protein.
On Tuesday, November 17, 2015 at 11:28:02 PM UTC+1, Nick R wrote:
-- The problem is the insane amount of calculation time you need to pour into getting the secondary structure just right. And with an enzyme 1Å makes all the difference.
Now there are RNA and even DNA catalysts, but they lack the flexibility of proteins. There are reactions they just can't do.
A marriage of the very predictable structures formed by DNA origami and the versatility of peptide chemistry is the short term solution I think.
DNA-based binding motives for a substrate of choice is to be found using SELEX. Around that one would engineer the scaffold to hold functional peptides via DNA-binding domains. Naturally, a covalent binding would be better, maybe somebody has an idea for this.
The DNA part of the structure would be more durable than regular enzymes. Peptide parts could be replaced constantly.
This DNAzymes could be used in environments that are to harsh for normal proteins, like industrial synthesis under high pressures and temperatures. They could be used together with cleaning agents or in low-moisture environments. Extending the DNA scaffold one could crystallize it easily while preserving functionality.
The reason you can't add metabolic functionality to a body is the reaction of its immune system to foreign proteins. DNAzymes could be deployed in the blood stream to serve custom reactions, given most of the peptide domains are derived from humans.
On Tuesday, November 17, 2015 at 11:28:02 PM UTC+1, Nick R wrote:
Recently, I've been very interested in the topic of completely human designed (de novo) proteins that are functional for a specific purpose, and decided to pose a question: If you could create any designer protein for a specific function, what would it's function be?
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