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.

ChemBE seminar focuses on cancer research innovation

The Department of Chemical and Biomolecular Engineering’s  scheduled Thursday, October 10 seminar will continue as planned at 3:30 PM in Maryland Hall 110. Jerry Lee, the Health Sciences Director at the National Cancer Institute (National Institutes of Health) will present his lecture “Advancing Convergence and Innovation in Cancer Research: National Cancer Institute Center for Strategic Scientific Initiatives (CSSI).”  A small reception will follow in Maryland Hall 109.

Jerry Lee

Jerry S.H. Lee, Ph.D

ABSTRACT

The National Cancer Institute (NCI) Center for Strategic Scientific Initiatives (CSSI) is a component of the NCI’s Office of the Director focused on emerging advanced technologies that have the potential of uniquely impacting the full spectrum of cancer basic and clinical research. The Center is tasked with planning, developing, executing, and implementing rapid strategic scientific and technology initiatives that keep the Institute ahead of the scientific curve with respect to potential new exciting areas and discoveries. This may involve direct development and application of advanced technologies, synergy of large scale and individual initiated research, and/or using available federal mechanisms to forge novel partnerships that emphasize innovation, trans-disciplinary teams and convergence of scientific disciplines. With an emphasis on complementing the scientific efforts of other NCI divisions, CSSI’s efforts seek to enable the translation of discoveries into new interventions, both domestically and in the international arena, to detect, prevent and treat cancer more effectively. This presentation will highlight various programs and their associated accomplishments within CSSI’s broad scientific portfolio of programs (Clinical Proteomic Tumor Analysis Consortium, Alliance for Nanotechnology in Cancer, Physical Sciences-Oncology Centers, Innovative Molecular Analysis Technologies, and Provocative Questions) and describe future directions and opportunities.

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.

Info sessions on international research internships

IMEC clean room

What’s better than working on a cool research project in your lab? Why it’s working on a cool research project in a fascinating European country, of course!

Johns Hopkins Institute for NanoBioTechnology offers undergraduate and graduate research internships at IMEC’s world-class nanofabrication laboratory in Belgium. Internships last approximately 10 weeks and include housing and a stipend. Find out how to apply and what kinds of projects are being sought at one of our upcoming informational sessions. Two sessions will be held October 8, one at 1 p.m. with light refreshments and a second at 5 p.m. with pizza, both in Croft Hall, Room 170.

RSVP is required to Tom Fekete at tfekete1@jhu.edu

Take a nanobreak at INBTea Time every Wednesday

Johns Hopkins Institute for NanoBioTechnology is pleased to announce the first INBTea Time every Wednesday in the corridor outside of our headquarters at 100 Croft Hall from 2:30 to 3 p.m. Grab a drink and a light snack. The first INBTea Time will be held on Wednesday, September 11. Enjoy a quick break and great conversation!

Screen Shot 2013-09-09 at 3.53.00 PM

Blog posts from Belgium

colin-leuven

Catholic University of Leuven (Photo by Colin Paul)

During the summer, a select group of researchers from Johns Hopkins travel to Leuven, Belgium to work at the micro- and nano- electronics fabrication laboratories of IMEC. Usually three to five students are able to go over for up to three months to work on a research project that is collaboratively arranged by both IMEC researchers and Johns Hopkins University faculty.

The students usually are advancing some aspect of a project they have started here at JHU. In a few instances, researchers from IMEC come to JHU to work. Faculty at both locations work together to develop projects that are mutually beneficial to all parties.

Johns Hopkins Institute for NanoBioTechnology provides financial support for our research through the National Science Foundation’s International Research Experience for Students (IRES) program. The arrangement with IMEC has been in place since 2009.

IMEC, which used to be referred to as the Interuniversity Microelectronics Centre, is an unusual research entity that grew out of an agreement between the Flemish government and the academic community at Catholic University of Leuven They now have more than 2,000 researchers from all around the globe working at their high tech facility.

To keep in touch with our researchers while they are away and to find out about their outside of laboratory adventures, INBT established the IMEC blog.  Click here to check out what our students have done, this summer and over the last several years.

 

Are cellular technologies scalable?

Are cellular technologies scalable? According to Phillip Vanek, Head of Innovation at Lonza Bioscience, the answer to this question is “yes”, but only if scaling is considered very early in the technology’s development. Vanek addressed the topic of scalability at his talk at the INBT symposium.

scalabilityScaling-up of bench-top science into industrial processes is difficult for a number of reasons. Commercial-scale production of cell-based products introduces regulatory challenges and production volumes never encountered on the bench scale. Even the basic laboratory chore of cell passage can become a large hurdle when attempting to grow large number of cells in the multi-layered cell factory system.

With such challenges in mind, Vanek lays out a number of ways to improve the success rate of scaling up processes. He stressed that a process should ideally be closed for maximum success. A closed process prevents product contamination and minimizes user error. Also, maximizing automation helps minimize operator error in processing.

Most importantly, the treatable patient pool sizes and dosage requirements need to be well-known for a process to be commercially successful. Vanek concluded that cellular technologies are scalable, but only if researchers start with end goals in mind early and are well-aware of potential pitfalls.

Lonza 

Editor’s Note: This a summary of one of the talks from the 2013 Nano-bio Symposium hosted by Johns Hopkins Institute for NanoBioTechnology held May 17. This summary was written by Christian Pick, a doctoral candidate in the chemical and biomolecular engineering laboratory of Joelle Frechette. Look for other symposium summaries on the INBT blog.