View Single Post
Jan28-12, 01:12 AM
Other Sci
Sci Advisor
P: 1,393
Quote Quote by gravenewworld View Post
To your first point, sure you can get a yeast to produce tons of your protein, can you control for EXACTLY how much protein your yeast produces? Probably not? With automated programmable syntehsise you can control exactly how much protein is in your solution and I imagine immune system response is a function to how much dose you give. Let's say you have a yeast cell produce your protein. Is it easy to count 10,000 proteins out of what it produces? What if you need 100,000 proteins? We're talking about personalized medicine. Everyone's immune system is different, with an automated synthesis you could theoretically fine tune the concentrations you need to produce a response correct?
If you have a large amount of purified protein it is trivial to measure out a certain quantity.

Could you create some sort of reactor to synthesize the peptide strand and have its end product "spit out" into a soup filled with features native to a cell environment such as chaperone proetins?
The ribosome is one such reactor... In fact, some recent studies suggest that features of the ribosome help to aid the folding of proteins to their native state. Although the primary sequence of proteins determines their structure and folding, in practice, it is pretty difficult to get large unfolded proteins to fold back into their native state.

I'm sure this sounds ridiculous, but I bet the atom bomb did too in the 1890s.
It's not completely ridiculous, but I'm just pointing out some potential problems with your idea. After all, if you can think of a solution to these problems, the idea won't be so ridiculous after all. Chemical synthesis makes it much more easy to add unnatural features to the protein you're synthesizing (such as unnatural amino acids, amino acids with the wrong chriality, sites for attachment of specific post-translational modifications, etc.), so it could definitely offer some advantages over recombinant expression.