Gaining perspective from an international research internship

I was fortunate enough to able to complete an internship abroad during my undergraduate career. Though I was extremely excited to begin work at a German university in Berlin, I was also very apprehensive about the huge transition I would have to make. Not only was I living in a new country speaking a relatively uncomfortable language, but it was also my first laboratory experience in the side of materials science, which so often overlaps with chemistry. Through my time in Berlin, I learned about German culture, conducting science abroad, and I got a healthy dose of chemistry.

Luisa Russell during her internship.

Luisa Russell during her internship.

My lab work in Germany involved the synthesis and functionalization of gold nanospheres and nanorods for the ultimate goal of the treatment of rheumatoid arthritis using hyperbranched polyglycerol. Though I worked under an older graduate student and had to start essentially from the beginning due to my relative lack of chemistry lab training, my fellow interns and I were given many opportunities to expand on our laboratory skills, and I came to be independent in both synthesis and in data collection and analysis for a variety of nanoparticles. Though we mainly worked with gold, we also explored more nontraditional nanomaterials including graphene and nanodiamonds through work my mentor was doing in collaboration with other groups, giving me a broad experience in nanotechnology.

In addition, doing my internship abroad rather than at another university in the United States gave me a new perspective on science as an international endeavor. Though lab books, conversation, and notes were in German, everything with a larger audience was conducted in English, from guest lecturers to group meeting presentations to papers written for publication in journals. While this made me a little more comfortable given my barely conversational German, it also struck me how my peers were obligated to be conversant in English to be part of the international science community, as well as a contributing part of their own local groups. This helped me understand the unique challenges faced by international scientists, and I look forward to continuing work with international collaborators in the future.

My internship, though it started out slow, ended up being an invaluable experience for my current work. It was a great way to get an in depth and low commitment experience with an aspect of lab work in materials science that I hadn’t previously been familiar with, and inspired me to continue working in this field. My work in the Searson Group centers around nanoparticle synthesis as applied to quantum dots, and my experience both as a member of a chemistry lab and as a semi-independent synthesizer of nanoparticles gave me an advantage in learning to navigate my way around the lab and the relatively difficult protocols applied in the synthesis of quantum dots. While it did break up the span of time over which I could do longer term research, ultimately the opportunity to explore a variety of aspects of materials science in a hands-on way was extremely valuable, and helped to inform my future research interests.

Luisa Russell is a second-year PhD candidate in the materials science department working on hybrid multifunctional nanoparticles in Peter Searson’s research group.

Academic research internships are for grad students too

Cell migration assays

Before enrolling in the PhD program in the Department of Chemical and Biomolecular Engineering at Johns Hopkins, I didn’t know that academic internships were available for graduate students. When I was an undergraduate, I spent one summer working at a Research Experience for Undergraduates (REU) program at Iowa State University. REU programs are paid research internships that are funded by the National Science Foundation (NSF) and hosted by universities throughout the country, and they are well-advertised by academic advisors. They provide great opportunities for undergraduate students to see what full-time research in an academic setting is like before committing to graduate school. My undergraduate research experiences were instrumental as I made the decision to apply to PhD programs.

However, I didn’t realize that similar opportunities would be available once I’d entered grad school. I was very excited to learn that INBT offers an International Research Experience for Students (IRES) program that is open to both graduate and undergraduate students. This program offers an incredible opportunity to work internationally. By partnering with the Inter-University MicroElectronics Centre (IMEC) in Leuven, Belgium, INBT gives students the chance to work in IMECs microfabrication facilities to develop biomedical devices. They have incredible fabrication facilities at IMEC, and students traveling there learn a lot about how microelectronics manufacturing techniques can be translated to answer biological questions.

Leuven pic-web

In July and August of 2013, I visited IMEC to work on using new imaging techniques to study cell migration. We are trying to make cell motility studies easy, affordable, and high-throughput. Time-lapse motility experiments are typically limited to labs focused on cell motility because they require expensive microscopes and specialized equipment. Therefore, not every lab that cultures cells can perform these experiments, even though tests of cell motility can tell researchers a lot about other cellular behavior.

At IMEC, I worked on using an affordable imager that could be placed directly in cell culture incubators to study cells in wound healing, random motility, microcontact printing migration, and microchannel migration assays. We had some promising early results, and our collaboration is continuing. The internship provided me exposure to techniques I wouldn’t have otherwise known about, and I learned a lot about building collaborations with other researchers.

Colin Paul is a fourth-year PhD student in the laboratory of Konstantinos Konstantopoulos in the Department of Chemical and Biomolecular Engineering and Institute for NanoBioTechnology.

Gerecht research featured in Baltimore Sun science section

Science journalism is coming back to The Baltimore Sun, or so it would seem. Evidence of this comes in the form of this well written article by Arthur Hirsch about work in the laboratory of Sharon Gerecht, associate professor of Chemical and Biomolecular Engineering and an affiliated faculty member of Johns Hopkins Institute for NanoBioTechnology.

Photo  from The Baltimore Sun.

Photo from The Baltimore Sun.

The Gerecht lab is working on ways to coax stem cells into becoming tiny micro blood vessels, the kind crucial to feeding nutrients to new or transplanted tissue. Without these smallest branches of blood vessel, tissue cannot thrive.

Hirsch does an excellent job at not only deftly reporting Gerecht’s findings but beautifully describing what the vessels look like and the overall significance of the work. But this is not a critique of Hirsch’s writing. I am unqualified to do that. What this IS, is a tip of the hat to The Baltimore Sun for a) actually having a science story that was about the work of local scientists and b) assigning an extremely competent writer to produce the work.

I say this, because for the last 10 years or so, there seems to have been a steady decline in science reporting in by local media. The decline was in the quantity as well as in the quality. The New York Times still had their Tuesday Science Times, and a few other major dailies have managed to keep their science sections alive. But overall, there was a sharp and rapid decline in science journalist positions at smaller newspapers. Entire departments were disassembled. Bureaus shut down. Science stories, if they were written, were about “news you could use” and were relegated to newbie writers, many of who had little or no scientific understanding. Many former science reporters moved into the blogosphere or took up public relations jobs, like I did.

But the Gerecht story was about basic science, not about some new gadget that could fix this or that right now. It was about the scientific process and “eureka” moments. It gave insight into how scientists work, and even more importantly, how LONG it takes to arrive at a significant finding. (In this case, it has taken Gerecht 10 years to arrive at these findings.)

Maybe there is hope for the future of science journalism at the local level yet.

Check out The Sun story here:

Lab-grown blood vessels made with less ado

Mary Spiro is the science writer and blog maven for Johns Hopkins Institute for NanoBioTechnology. All comments can be sent to mspiro@jhu.edu.

Definition: What is Brownian Motion?

Not all bumper cars are created equal. Somehow I always pick the one with a sticky gas pedal and become the object of torment for my opponents. This is essentially what happens to microscopic particles when you stick them in a jar of water. The microscopic particle is a massive bumper car stuck in the middle of the rink surrounded by a bunch of tiny super-charged bumper cars, water molecules. The water molecules are all crashing into the poor, defenseless particle at once, and this makes it move. If you were to watch the particle, it would look like it’s moving in random directions for no apparent reason. A botanist named Robert Brown (hence the name Brownian Motion) watched pollen grains doing this in water with a microscope almost 200 years ago.

Click on this image to watch "Dark Field Video Microscopy of 100 nm Gold Nanoparticles"

Click on this image to watch “Dark Field Video Microscopy of 100 nm Gold Nanoparticles” by Gregg Duncan

It turns out actually that this process isn’t entirely random. How fast particles jiggle around is dependent on a few things. As the particles get bigger, they will move slower because more water molecules have to gang up on it to push it around. We can also give the water molecules more energy by increasing the temperature. At higher temperatures, the water molecules will move around faster and bang into the particle with more force that will make the particle move more quickly. It’s also important what kind of fluid the particle is immersed in, as you may or may not know from experience, it’s a lot easier to swim through water then something more viscous, or “thicker” like molasses. So if you take these few things into consideration, we can predict how big the random jumps particles make pretty accurately.

So then how do we measure how fast they move? Well, you need some way to watch the particles move around and this is still done the same way Robert Brown did back in the day with a microscope. Then you can watch the particle for awhile and write down where it went over time. You’ll see that if given x amount of time, the particle on average moves about the same distance. In fact, if you plot the average distance the particle moves versus time, it’s a straight line. The slope of that line is what we use to figure out the diffusion coefficient of the particle, and this tells us how fast or slow the particles will move.

Luckily in my lab, we have fancy cameras attached to our microscopes to make movies of particles moving around. I have a video here I took recently of some gold particles I was messing around with. I used a technique called dark field microscopy, which is a nice way to image really, really tiny particles like these that can’t be seen in normal microscopes. We’ve also written particle tracking software that does all the number crunching for us to figure out how fast the particles are moving. It is important for us to know how fast particles are moving as they approach each other for instance, when we try to build crystals out of them or as they approach a surface, like a cancer cell.

Story by Gregg Duncan, a Ph.D. student in the Department of Chemical and Biomolecular Engineering with interests in nanoparticle-based biosensing and drug delivery.

Lindau 2013: Mingling with Nobel Laureates

During the first week of July 2013, 34 science Nobel Prize winners congregated on the island of Lindau, Germany to meet and mentor the next generation of leading researchers. 625 undergraduate, graduate, and postdoctoral students from 78 countries were invited to attend this exclusive meeting. I was very lucky to be among them!

The Lindau Nobel Laureate Meeting has been held annually since 1951 and rotates among the Nobel Prize categories of chemistry, physics, physiology and medicine, and economics. This year’s meeting was devoted to chemistry. The Lindau Mediatheque is a great resource for meeting lectures, abstracts, and programs. The database lists all of this year’s attending Laureates, along with the years and disciplines in which they won the Nobel Prize.

U.S. researchers explore the island city of Lindau, Germany.

U.S. researchers explore the island city of Lindau, Germany.

Conference mornings were spent in widely-attended and inspiring lectures by the Laureates, while the afternoons involved break-out sessions where we could asks the Laureates our questions in a more intimate setting. I learned the processes through which many of the Nobel-prize winning discoveries were made and where some of the Laureates were when they received the infamous phone call informing them that they had been awarded the Prize. The conference’s U.S. delegation consisted of approximately 70 graduate students, and our organizing partner, Oak Ridge Associated Universities, was able to score us some great additional interaction opportunities with a few of the Laureates. We had our own dinner parties arranged with Brian Kobilka (Chemistry, 2012) and Steven Chu (Physics, 1997, and former U.S. Secretary of Energy). I had the pleasure of sitting next to Akira Suzuki (Chemistry, 2010) during an extravagant international get-together dinner sponsored by the Republic of Korea.

A panel of Nobel Laureates and scientists discusses the importance of communication in science. Speaking in this photo is Ada Yonath (far left), who won the Nobel Prize for Chemistry in 2009 for her studies on the structure and function of the ribosome.

A panel of Nobel Laureates and scientists discusses the importance of communication in science. Speaking in this photo is Ada Yonath (far left), who won the Nobel Prize for Chemistry in 2009 for her studies on the structure and function of the ribosome.

The Laureates were treated like celebrities on the island of Lindau. They were each gifted their own luxury car for the week, and personal drivers shuttled them between conference events. Students vied for their pictures and autographs like they were rock stars! My favorite day of the conference incorporated a boat trip to Mainau, another German island in Lake Constance. The scenic two hour sail on a giant cruise ship included food, drink, and even dancing with the Laureates and their spouses. Once on the island of Mainau, we toured spectacular gardens and enjoyed an authentic Bavarian lunch.

From meeting science “superstars” to networking with students from around the globe and exploring a beautiful island city, I can’t speak highly enough of the remarkable experience. For information about how to apply to be a part of the U.S. delegation for the 2014 Lindau Meeting, which will focus on physiology and medicine, visit http://www.orau.org/lindau/.

Story by Allison Chambliss, who is entering her fifth year as a PhD student in the laboratory of Denis Wirtz in the Department of Chemical and Biomolecular Engineering.

 

What Does This Do? HPLC

Recently, I have been using a machine called a HPLC quite a lot in my research. This has lead to quite a lot of questions like, “What is an HPLC? What does it actually do?” mostly asked by my grandma.

So, HPLC stands for High-Performance Liquid Chromatography, which is a mouthful. One will also hear it referred to by an older term, High Pressure Liquid Chromatography. You can see why most scientists are lazy and just refer to it as HPLC.

Erin Gallagher at the HPLC.

Erin Gallagher at the HPLC.

What a HPLC actually does is force a liquid mixture, which you want separated, through a tube of packed beads (called a column) at high pressure. In this liquid mixture there is some component that you want to separate from the rest of the mixture, whether it is a protein you need purified after synthesis or a drug from a urine sample. This is how doctors monitor that you are getting the right dosage of a drug and one of the ways that cocaine and other illicit drugs are tested for1.

As the sample passes through the column certain components in the sample will be attracted to the packed beads. Those components will take longer to get through the column because they keep getting stuck to the beads as they go through the column. This means that some components in the mixture will fly through the column, while others will take much longer to get through the column because those components keep sticking to the beads and then unsticking. This process is how the HPLC separates the mixture into the different parts. The sample can be separated using size, polarity, or several other chemical properties.

A detector is attached at the end of the column to identify what is coming off the column when. The detector can use many different types of detection, from ultra violet/visible light to mass spectroscopy, to figure out what component of the mixture is coming off of the column at what time.

Overall, the HPLC helps scientist separate and identify, and sometimes even quantify, parts of a liquid mixture.

1) Heit et al. Urine drug testing in pain medicine. Journal of Pain and Symptom Management March 2004. Pages 260–267

http://www.sciencedirect.com/science/article/pii/S088539240300530X

For a more thorough walk through and some awesome diagrams of HPLC see:

Harris, Daniel C.. Exploring Chemical Analysis. 4th ed. New York: W. H. Freeman and Company, 2009. Print.

 

Erin Gallagher is a second year PhD student in Peter Searson’s Materials Science and Engineering lab.

Bee blight and a honeycomb of funding possibilities

by Holly Occhipinti http://www.flickr.com/photos/pinti1/5519458297/

by Holly Occhipinti http://www.flickr.com/photos/pinti1/5519458297/

Time Magazine had an issue recently where the front cover asked, “What would the world be like without bees”? (1) This might seem like a rather small loss to the global ecology; how could bees play that large of a role in our daily lives? Actually, bees are rather important for us as human beings and for our food sources. The article estimated that the loss of bee pollination of plants would cost several billion dollars annually. This is perhaps the reason why a funding source we as scientists might not be accustomed to thinking about, the U.S. Department of Agriculture through the Agricultural Research Services (ARS), is looking to fund research to protect bees. (2) I believe that this could provide a unique source of funding for labs interested in studying and preventing the spread of Bee Blight.

What is Bee Blight then and why is it threatening bees?  As the source from above writes, Bee Blight is a poorly understood phenomenon, which is causing a change in worker bee behavior to have them leave their hives.  This decreases the overall population of bees and the effectiveness of the bee hive at producing honey and pollinating.  It is speculated that a combination of pesticides and fungicides that are currently in use are somehow poisoning the honey bees and causing them to exhibit this strange behavior.  Due to the fact that this concepts is very poorly understood, there are a multitude of efforts being made to find solutions to the problem of Bee Blight.

We as scientists at Johns Hopkins University have an opportunity to help research this problem and, in terms of funding, gain access to the resources that the ARS and other groups is providing.  Recently, a Harvard Lab was provided almost ten million dollars from the NSF to study how to make a hive of robotic bees to replace the ones found in nature. (3)  As someone whose research project is based on studying Melittin, the key component of Bee Honey Venom, and who is also an amateur entomologist, I believe that the solution might not need to be that exotic.  How many of us work on nanoparticles that are supposed to have very specific properties in very specific environments?  How many of us work on creating coatings for devices that kill off bacteria and other harmful diseases?  How many of us work in the public health department and know the impact that proper food management has on people’s health?  I believe that there are many other options, from better crops to better pesticides, that we at Hopkins have the ability to investigate and that this provides a new source of funding for our efforts.

  1. Time Magazine, August 2013
  2. Kaplan K. (2013, March 7). Honey Bees and Colony Collapse Disorder.  ARS website. Retrieved 9/9/2013 from <http://www.ars.usda.gov/News/docs.htm?docid=15572>
  3. Robobees Lab. (2013). Home Page. Robobees Lab Website. Retrieved 9/9/2013 from <http://robobees.seas.harvard.edu/>

By Gregory Wiedman, a graduate student from the Materials Science Department who is altering natural peptides from Bee Honey venom to improve drug delivery.