Why everyone (including you) should care (at least a little) about what we do — Part I

Whether it be the sweeping eagle in his flight, or the open apple-blossom, the toiling work-horse, the blithe swan, the branching oak, the winding stream at its base, the drifting clouds, over all the coursing sun, form ever follows function, and this is the law.
Louis Sullivan, 1896

Architect Louis Sullivan looked at the animated world evident around him and concluded: Form follows function. 
 Much has happened since 1896. We are now able to probe much deeper into the inner workings of life and what we find is, that Sullivans statement holds true. Even for the most basic molecular work-horses we know: proteins.

Proteins are long strands made up of the 20 natural amino acids that are universal to every cell. Whether you are a tiny bacterium, trying to make a living off of hot volcanoes thousands of feet below the sea or a human being, analysing the newest stock market trends in downtown London: Both use those 20 amino acids to make up their proteins to keep their cells alive and working.

Proteins do everything. Even though they are strands and therefore rather two-dimensional in nature, they are able to fold into three-dimensional structures. It’s like tying a knot in a shoe string — the two-dimensional string gets a three-dimensional shape and a function — in this case keeping your shoes from falling off your feet.

A strand of amino acids folding into the three-dimensional structure of a protein

The form that proteins so take then determines their function. Some of them do chemical reactions in your body, like the ones who help you to convert sugar into energy — those are called enzymes. Others are able to recognize and bind to invading bacteria and viruses thus alerting your immune system — these are called antibodies. The image below shows the three-dimensional structure of an enzyme and an antibody. Again, form follows function: There are distinct areas responsible for the proteins function.

The three-dimensional structures of an enzyme and an antibody. They have defined areas that are crucial for function.

Would it surprise you if I told you that these two proteins are responsible for a global market worth around 100 billion dollars? 
 The sugar-converting enzyme is used in glucose biosensors which help millions of diabetes patients to monitor their blood sugar levels and thus live with their illness. 
 Antibodies are used as drugs that help against cancer, autoimmune diseases and of course infectious diseases.

Proteins are amazing. But they could be even more amazing. Antibodies that can recognize and bind to cancer show immense promise as a delivery helper for chemotherapeutic drugs. This would mean that the toxic drugs responsible for the awful side effects in chemotherapy would be delivered directly to the cancer, thus eliminating the side effects of chemotherapy. 
 Similarly, biosensors could be used not only to easily measure blood sugar levels but everything from environmental toxins in your home to your drug levels thus informing you when to take your next treatment for optimal medication impact and safety.

There is a reason why this isn’t happening as fast as we would like to see it. Proteins have an inherent flaw. They are really difficult to attach things to in a controlled manner. Biosensors need enzymes to be attached to a surface so that we can measure their change when they encounter the substance they are detecting.

And if we want to haul drugs specifically only to cancerous tissue they must be attached strongly to the antibody to avoid damage elsewhere in the body.

Form follows function. That also means that there are areas on a protein that we shouldn’t meddle with because they are important for function. We are therefore forced to attach things to proteins at defined sites where the attachment doesn’t impair function. But we are not able to do that very well in a cost-efficient manner.

The areas responsible for function can not be used for attaching things without losing function.

Until now.

The answer to “How?” is coming up in our next blog post. Stay tuned :)