Because its name sounds like a vintage fighter plane, one might think the “Heme Team” that works with this enzyme is a group of pilots or aviation mechanics. But P450 (short for Cytochrome P450) refers to a family of enzymes that do vital work in the human body such as clearance and transformation of pharmaceutical drugs in the liver. And the “Heme Team” (named for heme, an iron-containing chemical component in all members of the P450 family) are four student research assistants working this summer in the chemistry lab of Professor Laura Furge. The team includes Rina Fujiwara ’15 (pictured at left), Amanda Bolles ’14, Mara Livezey ’13, and Parker De Waal ’13.

According to Fujiwara, Cytochrome P450 2D6—one member of the enzyme family—is responsible for the metabolism (think: conversion into a useful form) of some 20 percent of the medicines we take. So it’s definitely a P450 worthy of study—which, of course, means nature made it difficult to grow in a laboratory setting (as sure as the vegetables your mother said were good for you always tasted terrible). In fact, a great many P450 enzymes are intriguing, and the chemical modification of them and their mutations could one day have significant application in making medicines more effective.

Enter the Heme Team. Part of its summer work, says Fujiwara, has been to use recombinant bacteria (bacteria modified to include the DNA of P450 2D6) to grow the enzyme. Then team members try to separate the purified enzyme from the bacterial culture. Last year, they came close to achieving the goal. This year they developed a new protocol in which the bacteria cells (think: P450 factories) grow more slowly. Fujiwara is also doing work to obtain an even more difficult to express mutant version of 2D6, and that work might become the basis of her Senior Individualized Project next year.

On the threshold of her third year at K, the international student from Japan (chemistry major and thinking about a second major in biology) has always loved science, particularly the area of nutrition. This is her first year in the Furge lab, and she loves working with Dr. Furge and her fellow research assistants. “They are great mentors,” says Fujiwara, “and always help me with my many questions, no matter how elementary those questions may seem.” One exciting side effect of her work this summer, she adds, is the enthusiasm it has sparked for cell biology and biochemistry, two courses she is eager to take during her junior year.

Another great side effect is Dr. Furge’s expertise in another kind of chemistry—baking! “She makes delicious carrot cake and blueberry pies and brings them in for her research students,” says Fujiwara. “I love this lab!”

During the second summer of research on her Senior Independent Project (SIP), chemistry major Virginia Greenberger (pictured at left) is spending more time in method development than data collection. Here’s the thing about that: “We’ve never done this work before,” says Greenberger. (The other member of “we” is her SIP supervisor, Professor of Chemistry Regina Stevens-Truss; they are trying to develop a method to determine how certain protein pieces—called peptide sequences—kill bacteria.) That “never-having-done-this-work-before” means her SIP research is on the far edge of new discovery, which makes it very cool. But it can also be very frustrating—just one example: the peptide sequences are “sticky” and prone to clump, which makes methods to effectively study them more difficult to develop.

Some back story, which goes back further than last summer. About a decade and a half ago, Stevens-Truss noticed that bacteria she’d altered to produce a certain peptide were being killed by that peptide. Very interesting discovery, on hold for a dozen or so years. Then last summer Stevens-Truss and Greenberger began to study in earnest the protein components responsible for killing the bacteria. These peptide sequences are spiral in shape and carry a positive charge. Shape and charge are matters of chemistry and potential chemical alteration. Summer number one focused on which peptide sequences were the most effective killers of which kinds of bacteria–gram positive (Staph aureus, for example) and gram negative (E-coli, for example). The research team devised a method that uses light to determine the degree to which various peptide sequences inhibit various bacteria. Roughly speaking, “cloudy” or opaque solutions (that block light) mean the bacteria are not much affected by the peptide sequence, but a clear solution indicates significant antibacterial activity. The research could eventually prove very important. Ours is an age of antibiotic resistance. Certain bacteria cause serious infectious diseases, but their reproduction rate (combined with human misuse of antibiotics) selects for resistant strains.

Summer two’s work seeks to repeat (and confirm) the results of last summer and determine how the effective bacterial assassins do their work. How does one determine that? Greenberger is currently working on a method that infuses liposomes with dyes. Liposomes are bag-like structures whose membranes mimic the membranes of cells. A killing mechanism by which the spiral-shaped peptide sequences drill through bacterial cell membranes would be suggested if the liposome look-alikes suddenly release their dyes. That’s the method on which Greenberger was currently at work at the time of this interview. The working title of her SIP is “Studying Antibiotic Action of Peptide Sequences containing a Cationic Amphipathic Helix Structure.” But that could change, depending on that ever-changing ratio of “cool” to “frustrating.”