The Slick Joint

English
 
Body joints are superbly lubricated. Wherever two bones meet in our body, joints allow us to grasp, bend over, run or dance - and they’re supposed to last a lifetime.

Mimicking key design elements of this biolubrication system, physicist Prof. Jacob Klein of the Materials and Interfaces Department has recently created a synthetic lubricant that cuts friction a thousand-fold or more. The study, published in Nature, could lead to a range of applications - from longer-lasting micro-machines to biomedical products.

Previous studies had suggested that biolubrication systems, such as those in joints and eyes, maycontain hyaluronan molecules that coat the rubbing surfaces, shielding them from mechanical damage. Hyaluronan was also known to be strongly attracted to water.

Klein and his colleagues suspected that in joints, hyaluronan may be attached to a thin cartilage layer covering the bone. Parts of the long, chain-like hyaluronan molecule stick out into the synovial fluid between the bones, resembling bristles on a brush.

The team developed a synthetic model that mimicked a double-brush system, anchoring two charged molecules (polyelectrolytes) to opposite-facing ceramic surfaces. The resulting system showed extremely effective friction resistance, particularly when exposed to a water-based solution. “The brushes strongly try to avoid each other, resisting contact even when an external force is applied to press them closer. This enables them to easily slide past one another,” says Klein.

The synthetic brushes were designed to imitate the electrically charged nature of biolubricants. The negative charge on the bristle tips then attracted water molecules - which in fact explains why the brushes performed most effectively in a water-based solution. “The water molecules are tightly bound by the charges, causing them to act like molecular ball bearings,” Klein explains.

Prof. Klein is the incumbent of the Hermann Mark Professorial Chair of Polymer Physics.

Lubricating actions: Water molecules (H20) bind tightly to charges on brushes, acting as molecular ball bearings

 

Water molecules (H20) bind tightly to charges on brushes, acting as molecular ball bearings
Chemistry
English

Wet Scans

English
 
The scanning electron microscope (SEM) has been a basic research tool for 50 years, and for all of those years scientists have been looking for better ways to observe biological samples under its beam. The problem is that biological samples cannot withstand the vacuum inside the SEM. Procedures used today include coating the specimens with an ultra-fine layer of gold, quick-freezing samples in special deep-freezes or treating them with drying solvents.

The scanning electron microscope (SEM) has been a basic research tool for 50 years, and for all of those years scientists have been looking for better ways to observe biological samples under its beam. The problem is that biological samples cannot withstand the vacuum inside the SEM. Procedures used today include coating the specimens with an ultra-fine layer of gold, quick-freezing samples in special deep-freezes or treating them with drying solvents.

Now Weizmann Institute researchers have found a way to view samples of biological materials in their natural, “wet” state. The secret lies in producing a very thin but tough polymer capsule to enclose the sample. Dr. Ory Zik, who developed the capsule with Prof. Elisha Moses of the Physics of Complex Systems Department, says: “We came across the capsule material while researching applications for semiconductor industry techniques in the life sciences’ SEMs.”

The capsule’s polymer is unique in that it allows the electrons with which an SEM works to pass through unobstructed, giving scientists a clear view of what lies inside, without the use of tricky, tissue-distorting procedures. Researchers hope the new method will advance the study of such biological materials as lipids, which are easily destroyed by other preparation methods.

The finding was recently published in the Proceedings of the National Academy of Sciences (PNAS), USA. Zik, in cooperation with Yeda, the business arm of the Weizmann Institute, has founded a company, called QuantomiX, based on the technology.
 
Prof. Moses’ research is supported by the Clore Center for Biological Physics and the Rosa and Emilio Segre Research Award.
Technology & Applications
English

Gaining Momentum

English
 
An accidental discovery 40 years ago led to an improvement in firefighting techniques: When polymers (long chains of molecules) were added to the water pumped through firehoses, that water projected over greater distances - of critical importance to those living and working in high-rise buildings.

But the why behind this finding remained a mystery until it was recently solved by a group of scientists of the Weizmann Institute’s Chemical Physics Department that included Prof. Itamar Procaccia, Dr. Victor L’vov, Dr. Anna Pomyalov and postdoctoral fellow Dr. Vasyl Tyberkevych.

Intuition told them that adding polymers should slow the flow of water through the hose by raising the water’s viscosity. The scientists noted that the normally folded up polymer molecules became stretched out like long strings of beads in the rushing stream, which did, indeed increase water viscosity.

However, a stronger counter-effect was also noted. The pressure produced in the pumps creates momentum, some of which carries water out of the end of the hose and some of which flows to the pipe walls. The polymers interfere with the flow of momentum to the pipe walls, and since the total momentum in the hose remains constant, a reduction in flow of momentum in one direction increases it in the other. The effect, therefore, is to raise the momentum, and thus the speed, of the water exiting the hose.

Institute scientists are currently testing the possibility of replacing the long-chain polymers with tiny air bubbles, an approach that may have relevance for transporting oil in pipelines and reducing drag on the bows of ships.
 
Prof. Procaccia’s research is supported by the Minerva Center for Nonlinear Physics of Complex Systems; the Naftali and Anna Backenroth-Broniki Fund for Complexity established by Mr. Yehuda Broniki of Israel; and the late Mr. Simon Pupko. He is the incumbent of the Barbara and Morris L. Levinson Professorial Chair in Chemical Physics.
Chemistry
English

Twitching Whiskers Tell All

English

Our fingers run over surfaces; our eyes are in constant motion. This is all part of “active sensing,” key principles of which have now been uncovered by the team of Prof. Ehud Ahissar of the Neurobiology Department.

We intuitively understand that fingers moving upon surfaces should provide the brain with information very different from that acquired by merely touching a surface without movement, yet experiments have nearly always kept the organs stationary. Working with doctoral student Marcin Szwed and Dr. Knarik Bagdasarian, Ahissar tracked neuron transmissions of rats’ whiskers, which sweep back and forth to locate objects in their immediate vicinity, and thus are an ideal tool for studying the active aspects of perception. They found that two previously unknown basic types of neurons came into play. The first, which they called whisking neurons, responds solely to the whisking motion itself, even if the whiskers don’t touch an object. The second, which they dubbed touch neurons, informs the brain about the surface being touched. The scientists were able to discern subtypes in the second category, which came into play during different stages of contact. Ahissar’s team published these results in Neuron

Prof. Ahissar’s research is supported by the the Carl and Micaela Einhorn-Dominic Institute for Brain Research; the Nella and Leon Benoziyo Center for Neurosciences; the Abramson Family Foundation; the Edith C. Blum Foundation; the Irving B. Harris Foundation; and Mrs. Esther Smidof, Switzerland. He is the incumbent of the Helen and Sanford Diller Family Professorial Chair in Neurobiology.
Life Sciences
English

Live Footage of Enzymes

English

Thanks to a new method developed by the team of Prof. Irit Sagi of the Structural Biology Department, reality TV has reached enzyme molecules. They can now be viewed “live” in video clips. The clips’ resolution is so high that it is possible to see the movements of individual atoms within the molecule. Until now, scientists who studied the ultra-small enzymes had to rely on still photos. The pioneering method was published in Nature Structural Biology, where it was hailed as the first of its kind.

Apart from “putting enzymes on film,” the Weizmann Institute team was able to capture the step-by-step process an enzyme goes through as it performs its work. The entire process takes place in a fraction of a second. This new capability presents a huge step forward in the area of drug design, since it enables scientists to identify the precise parts of a molecule that are active in binding to a drug. Sagi’s team is doing just that for one enzyme family (called MMP), known to play a role in cancer metastasis. Using the knowledge gained by the new technique, the team has designed a molecule that blocks MMPs at a crucial phase. 

Prof. Sagi’s research is supported by the Avron-Wilstatter Minerva Center; the Helen and Milton A. Kimmelman Center for Biomolecular Structure and Assembly; the Ceil and Joseph Mazer Center for Structural Biology; the Cymerman-Jakubskind Prize; the Laub Fund for Oncogene Research; Prof. Clotilde Pontecorvo, Italy; and Verband der Chemischen Industrie.
Chemistry
English

Weizmann Wins International “Pretend Experiment”

English

More than 2,000 physicists from about 50 countries are preparing for an experiment, planned for 2007, which aims to find a particle believed to make up all mass in the universe. Proving the existence of the particle, called the Higgs, would improve our understanding of the universe and might open the door to “new physics,” the laws of which physicists today can only try to imagine.

The particle accelerator being built for this goal on the French- Swiss border will contain a particle detector, called ATLAS, which will receive more data at any given moment than all of the world's telephone networks combined. The big challenge will be to interpret the data. Thus the organizers of the project decided to conduct a “dry run”: Several small hints for a possible new physics were hidden among millions of simulated events, and groups of physicists were challenged to find as many hints as possible and “publish” their findings. Tying for first place were the Weizmann Institute and Cambridge University. The prize was a wooden brainteaser.

Taking a major part in the deciphering were Ph.D. student Arie Melamed-Katz, Profs. Ehud Duchovni and Eilam Gross, postdoctoral fellow Dr. Michael Rivline and Ph.D. students Lidija Zivkovic and Peter Renkel. 

Prof. Duchovni’s research is supported by the Nella and Leon Benoziyo Center for High Energy Physics.
Space & Physics
English

Resilience by Improvisation

English

Our cells can copy DNA even when it is severely damaged. Prof. Zvi Livneh and Ph.D. student Ayelet Maor-Shoshani of the Biological Chemistry Department inserted a foreign material - similar to that making up crude oil - into the DNA of the bacterium E. coli. To their surprise, the cell’s copying machinery was able to proceed unhindered.

The millions of cells that divide every day in the body do so by copying their DNA. This crucially important function, which enables the body to replace old cells and pass on genetic information from generation to generation, is performed by molecules called DNA polymerases. The new Weizmann Institute study shows that they are able to improvise to achieve their goal.

The scientists found that upon reaching the foreign material, the DNA polymerase stops working and a specialized DNA polymerase jumps in to rescue the stuck replication process. The latter is able to continue the copying process by inserting “nonsense” genetic components into the copy, much like a singer who forgets a few words and continues to sing by making up new ones. In other cases, the specialized DNA polymerase simply skipped over the foreign material or deleted it and was thus able to continue copying as usual.

These findings, published in Proceedings of the National Academy of Sciences (PNAS), USA, shed light on how the copying process is affected by damaged DNA. “They show the remarkable capacity of a cell to reproduce,” says Livneh, “and make one hopeful that even if extreme types of chemicals are accidentally introduced into our DNA, the body will be able to manage.” 

Prof. Livneh’s research is supported by the M.D. Moross Institute for Cancer Research; the Levine Institute of Applied Science; the Dr. Josef Cohn Minerva Center for Biomembrane Research; the Dolfi and Lola Ebner Center for Biomedical Research; and the J & R Center for Scientific Research. He is the incumbent of the Maxwell Ellis Professorial Chair in Biomedical Research.
Space & Physics
English

Nerves, Heal Thyselves

English

In a study published in Neuron, Weizmann scientists have now shown how neurons in the peripheral nervous system “raise the alarm” following injury, sparking a rescue process.

Nerves in the peripheral nervous system (any part of the body aside from the brain and spinal cord) are capable of regenerating, though they often do so poorly or slowly. A better understanding of how they regenerate could advance the treatment of injuries to the peripheral system (such as loss of sensation). It might also provide insights into fixing neurons in the central nervous system.

Nerve cells are uniquely shaped, consisting of a cell body and “arm-like” protrusions that transmit information to the cell (dendrites) and from it (axons). Axons can reach up to one meter in length in humans and are the main conduit for neural communication throughout the body.

Dr. Michael Fainzilber and Ph.D. students Shlomit Hanz and Eran Perlson of the Biological Chemistry Department found that a special protein called importin beta is produced in axons upon injury. This protein binds, among others, to components of a “healing message.” The whole group fastens itself to an “engine” called dynein that chugs along tracks leading from the axon to the nucleus. The group then enters the nucleus, alerting the cell to the problem and initiating nerve regeneration. 

Dr. Fainzilber’s research is supported by the Y. Leon Benoziyo Institute for Molecular Medicine; Mr. and Mrs. Alan Fischer, Larchmont, NY; the Abisch Frenkel Foundation for the Promotion of Life Sciences; the Irwin Green Alzheimer’s Research Fund; and the Buddy Taub Foundation. He is the incumbent of the Daniel E. Koshland Sr. Career Development Chair.
Space & Physics
English

Stem Cells On Call

English
 
They still don't have a personality and they're waiting for the maturity call. Stem cells in our bone marrow usually develop into blood cells, replenishing our blood system. However, in an emergency, the destiny of some of these stem cells may change: They can become virtually any type of cell – liver cells, muscle cells, nerve cells – in response to the body's needs.
 
Prof. Tsvee Lapidot and Dr. Orit Kollet of the Weizmann Institute's Immunology Department have found how the liver, when damaged, sends a cry for help to these stem cells. They discovered that certain molecules governing normal development of the liver become overproduced when it is damaged, signaling to the stem cells in the bone marrow to come to the site. The scientists were able to pinpoint the signaling molecules and describe the homing process.
 
The findings could lead to new insights into organ repair and transplants, especially liver-related ones. They may also point to a whole new stock of stem cells that can, under certain conditions, become liver cells. Until a few years ago, only embryonic stem cells were thought to possess such capabilities. Understanding how stem cells in the bone marrow turn into liver cells could one day be a great boon to liver repair as well as to stem cell research and therapy.
 
Prof. Lapidot's research was supported by the M.D. Moross Institute for Cancer Research; the Concern Foundation, Beverly Hills, CA; Ms. Rhoda Goldstein, Nanuet, NY; the Levine Institute of Applied Science; Ms. Nora Peisner, Hungtington, MI; and the Gabrielle Rich Center for Transplantation Biology Research.
Life Sciences
English

Deciphering Gaucher's Disease

English
 
An interdisciplinary team of Weizmann Institute scientists has solved the 3-D structure of an enzyme involved in Gaucher's disease, a genetic illness that mainly affects Ashkenazi Jews. The study, published in EMBO Reports, may lead to the design of effective new therapies.
 
Gaucher's disease is characterized by swelling and enlargement of the spleen and liver and disruption in the function of these organs; in rare cases, it may also affect the brain. It is caused by the accumulation of a fatty substance, or lipid, called glucosylceramide. Accumulation occurs due to a defect in the enzyme charged with breaking down this lipid and regulating its amount.
 
Today thousands of Gaucher's patients are treated by injections of this enzyme, in an approach called enzyme replacement therapy, or ERT. The annual cost of the therapy is approximately $100,000 to $300,000 per patient. More affordable alternatives, such as the ones that may emerge from the Weizmann Institute study, are urgently needed.
 
The Institute team included Prof. Tony Futerman of the Biological Chemistry Department, Prof. Joel Sussman of the Structural Biology Department and Prof. Israel Silman of the Neurobiology Department, as well as Dr. Michal Harel, Lilly Toker and graduate student Hay Dvir.The solved enzyme structure may help in the design of a more effective enzyme that would improve today's ERT. It may also make possible the design of small molecules that will supplement the damaged enzyme in the patient's body, thereby restoring its normal functioning.
 
Prof. Futerman's research was supported by the Estate of Ernst and Anni Deutsch-Promotor Stiftung, Switzerland; the Paul Godfrey Foundation; the Buddy Taub Foundation; the Sir Siegmund Warburg's Weizmann Trust; and the Estate of Louis Uger, Canada. He is the incumbent of the Joseph Meyerhoff Professorial Chair of Biochemistry.
 
Prof. Silman's research was supported by the Nella and Leon Benoziyo Center for Neurosciences; the Charles A. Dana Foundation; the Carl and Micaela Einhorn-Dominic Brain Research Institute; and the Helen & Milton A. Kimmelman Center for Biomolecular Structure & Assembly. He is the incumbent of the Bernstein-Mason Professorial Chair of Neurochemistry
 
Prof. Sussman's research was supported by the Charles A. Dana Foundation; the Jean and Jula Goldwurm Memorial Foundation; Mr. Yossi Hollander, Israel; the Helen & Milton A. Kimmelman Center for Biomolecular Structure & Assembly; the Joseph and Ceil Mazer Center for Structural Biology; the late Sally Schnitzer; and the Kalman & Ida Wolens Foundation. He is the incumbent of the Morton and Gladys Pickman Chair in Structural Biology.
 
The research utilized infrastructure provided by the Kekst Family Center for Medical Genetics.
Life Sciences
English

Pages