2018 Nobel Prize Winners for Their Work with Proteins and Enzymes

   
      Last week was a momentous occasion for many people in the field of research, as the Nobel's Prizes for each category were announced. Many people waited and watched, riddled with anticipation, as each winner was announced, and by Monday there were a grand total 12 Nobel Laureates recognized for their outstanding achievements. Among the 12 Nobel prize winners, there were 3 laureates of particular interest that contributed further to the knowledge and understanding of biology and genetic evolution.
     Dr. Frances H. Arnold was the first Nobel laureate to be recognized for her work with directed evolution of enzymes. Dr. Arnold pioneered the first bio-engineering method in 1990 called directed evolution. Directed evolution is a method that introduces random mutations into a gene, which is then inserted into an enzyme and is used as a template to produce a catalyst for desired reactions. Directed evolution has been used to produce chemicals that are safer for people as well as the environment. Chemicals such as bio-fuels, medicine, laundry detergents and more have been created using this process. Dr. Arnold has used evolution to her advantage and in an article in the NY Times she stated "I copied nature’s inventions, this wonderful process of evolution, to breed molecules like you breed cats and dogs.”

       Dr. George P. Smith and Sir Gregory P. Winters shared the 2018 Nobel Prize with Dr. Arnold for their work with bacteriophages. Dr. Smith, from University of Missouri, was looking to identify unknown genes using peptides and bacteriophages. In order to identify the unknown genes, Dr. Smith would insert genes into bacteriophages, which would then express the protein on the surface. Dr. Smith watched these antibodies to see if they would interacted with the proteins and identifying them as a pathogen. The different types of antibodies only fit specific types of proteins, and once an antibody identifies a protein, scientists can then deduce the identity of the unknown gene.
     Sir Gregory P. Winters, from MRC Laboratory of Molecular Biology UK, went a step further and used Dr. Smith's research to produce more efficient and prolific antibodies. Instead of inserting an unknown gene into a bacteriaphage, Dr. Winters inserted the bacteriapages with antibodies and selected the ones that bound the most effectively. He then repeated the process several times to produce powerful disease fighting antibodies. According to the NY Times, "the first antibody drug developed this way, adalimumab, which is sold under the brand name Humira" (Chang, 2018). This drug was used to fight diseases like rheumatoid arthritis, psoriasis and inflammatory bowl disease. In addition to his drug synthesis, Dr. Winter also used this technique to produce efficient antibodies that could shrink tumors in the human body. In order to do this, Dr. Winter tweaked a mouse antibody, using the same technique, and injected that antibody into a patient with a deadly tumor. The tumor shrank successfully and the patient suffered from no side effects. The shrunken tumor was the first ever human test to see if this procedure could be used for the public health.

Complex Life's First Milestone

Hydrothermal vent at the bottom of the ocean

     In regards to the origins of complex life forms, one theory is globally accepted. This is the theory that RNA strands were being continuously formed in the mixing pot that was the prehistoric ocean. These strands would grow and reproduce until longer, more complex chains formed actual life-forms such as early amoebas and worms. Scientists have now discovered how it may have been possible that complex RNA strands out-competed simple, shorter ones.

     Technically speaking, shorter RNA strands can reproduce more efficiently because, although they are more primitive, with less material to copy the process is quicker. However, an article in Science Magazine claims that pores in the rocks surrounding hydrothermal vents in the oceans floor may have created the perfect breeding ground for the complex RNA strands, that eventually lead to us. The superheated water that emerges from these fissures is highly enriched with nutrients. Through a physical effect known as thermophoresis, “charged molecules in a solution accumulate in colder water, and the longer chains, having more charge, would do this more often than shorter chains”. Add this save haven, porous environment, together with the flow of nutrients and temperature changes from hydrothermal vents, and the result is much more efficient reproduction.

     This theory was recreated in a laboratory experiment that resulted in the longer strands reproducing much better inside the pores, leading to larger and more stable populations. The new findings may have opened a door to better understanding the evolution and origins of complex life, and the environments that made it possible.  

Cured From the Inside Out

When we think about chemistry, the image that usually comes to mind is some sort of laboratory with bubbling, colorful substances in every-sized flasks over an ancient-looking Bunsen burner. We think of fume hoods with chemicals we probably shouldn’t be inhaling and little glass vials that probably should be labeled. We think of a traditional chemistry lab. However, an article recently published in ScienceDaily has a new, different image of chemistry…chemistry done within the laboratory of the human body.



A newly founded field of chemistry, by Carolyn Bertozzi, Ph.D., has started to emerge for the past decade known as bioorthogonal chemistry. First emerging from her study of viewing a virus entering a cell with fluorescent probes, its focus is a new form of drug development where chemical ingredients are added separately into the body where they eventually meet up at a designated point, create a reaction, and cure the patient. How is this different from other, pre-made oral drugs? Sometimes the oral drugs never reach the goal location strong enough to make an effect on the diseased tissue targeted. With this new method, the numerous ingredients, just like in a laboratory setting, are added separately, with each keeping their strong concentrations. Then, at a given point, they come in contact with one another, and a reaction occurs to produce the desired drug within the patient’s body.

However, as exciting as this may sound, it’s a bit trickier than it seems. In a lab, the conditions are easily controllable. (Ex. Temperature, timing, light exposure, cleanliness, etc.) In the human body, things are not quite so black and white. It’s more of all gray. There are different compounds, chemicals, and water all over the place, with little controls. Plus these chemists are restricted to reactions that can only occur in water, having the pH of 7, and at body temperature. After fighting through all of these obstacles, only then can the drugs begin to be made within the body.