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Nanoparticle Cluster Manufacturing Technique Using DNA Binding Protein Developed
Professor Hak-Sung Kim of the Department of Biological Sciences at KAIST and Yiseul Ryu, a doctoral candidate, used the Zinc Finger protein that specifically binds to target DNA sequence to develop a new manufacturing technique for size-controllable magnetic Nanoparticle Clusters (NPCs). Their research results were published in Angewandte Chemie International Edition online on 25 November 2014.
NPCs are structures consisting of magnetic nanoparticles, gold nanoparticles, and quantum dots, each of which are smaller than 100 nm (10-9m). NPCs have a distinctive property of collectivity not seen in single nanoparticles.
Specifically NPCS differ in physical and optical properties such as Plasmon coupling absorbance, energy transfers between particles, electron transfers, and conductivity. Therefore, NPCs can be employed in biological and medical research as well as the development of nanoelectric and nanoplasmon devices.
To make use of these novel properties, the size and the composition of the cluster must be exquisitely controlled. However, previous techniques relied on chemical binding which required complex steps, making it difficult to control the size and composition of NPCs.
Professor Kim’s team used Zinc Finger, a DNA binding protein, to develop a NPCs manufacturing technique to create clusters of the desired size easily. The Zinc Finger protein contains a zinc ion and specifically recognizes DNA sequence upon binding, which allows the exquisite control of the size and the cluster composition. The technique is also bio-friendly.
Professor Kim’s team created linear structure of different sizes of NPCs using Zinc Finger proteins and three DNA sequences of different lengths. The NPCs they produced confirmed their ability to control the size and structure of the cluster by using different DNA lengths.
The NPCs showed tripled T2 relaxation rates compared to the existing MRI contrast media (Feridex) and effectively transported to targeted cells. The research findings show the potential use of NPCs in biological and medical fields such as MRI contrast media, fluorescence imaging, and drug transport.
The research used the specific binding property of protein and DNA to develop a new method to create an inorganic nanoparticle’s supramolecular assembly. The technique can be used and applied extensively in other nanoparticles for future research in diagnosis, imaging, and drug and gene delivery.
Figure 1. A Mimetic Diagram of NPCs Manufacturing Technique Using DNA Binding Protein Zinc Finger
Figure 2. Transmission Electron Microscopy Images showing different sizes of NPCs depending on the length of the DNA
2014.12.04 View 11898 -
Thomson Reuters Nominates Distinguished Professor Ryong Ryoo for Its 2014 Nobel Citation Laureates in Chemistry
The Intellectual Property & Science business of Thomson Reuters announced on September 25th its “2014 Citation Laureates,” a list of candidates considered likely to win the Nobel Prize in the fields of physics, chemistry, physiology or medicine, and economics. The annual Thomson Reuters Citation Laureates will be recognized in perpetuity as contenders for a Nobel Prize.
Distinguished Professor Ryong Ryoo of the Department of Chemistry, KAIST, has been nominated for the 2014 Thomson Reuters Citation Laureates in Chemistry. He is the first Korean scientist who has made the list. In addition to Professor Ryoo, seven other scientists were selected as possible contenders for the 2014 Nobel Prize in Chemistry, or in the future.
Professor Ryoo was named alongside Charles T. Kresge, Chief Technology Officer of Saudi Aramco, Dhahran, and Galen D. Stucky, Professor of the Department Chemistry and Biochemistry at the University of California, Santa Barbara, for their research on the design of functional mesoporous materials (http://sciencewatch.com/nobel/2014-predictions/chemistry-laureates). Mesoporous materials have high surface areas with narrow pore-sized distribution and tunable pores diameters, offering promising properties and applications in various areas including adsorption, separation, sensing, and catalysis.
Professor Ryoo has focused his research interest in the synthesis of new functional nanoporous materials such as hierarchical zeolites, mesoporous silicas, carbons, and organic-inorganic composite materials that can be used for advanced applications in the production of alternative energy sources and in green chemical processes.
According to the press release by the Thomson Reuters, the list of the 2014 Nobel predictions includes 27 researchers representing 27 distinct academic and research organizations across nine different countries.
The annual Thomson Reuters Citation Laureates study is based on the analysis of proprietary data from the research and citation database, identifying the most influential researchers in the categories of chemistry, physics, physiology or medicine, and economics. Since its inception in 2002, the study has accurately forecasted 35 Nobel Prize winners. For the full text of the press release, please go to: http://thomsonreuters.com/press-releases/092014/2014-nobel-laureates-predictions.
2014.09.29 View 11213 -
News Article on the Development of Synthesis Process for Graphene Quantum Dots
Before It's News, an international online news agency, highlighted the recent research conducted by KAIST professors (Seokwoo Jeon of the Department of Materials Science and Engineering, Yong-Hoon Cho of the Department of Physics, and Seunghyup Yoo of the Department of Electrical Engineering) on the development of synthesis process for graphene quantum dots, nanometer-sized round semiconductor nanoparticles that are very efficient at emitting photons. If commercialized, this synthetic technology will lead the way to the development of paper-thin displays in the future.
For the article, please go to the link below:
Before It’s News, September 3, 2014“Graphene quantum dots prove highly efficient in emitting light”
http://beforeitsnews.com/science-and-technology/2014/09/graphene-quantum-dots-prove-highly-efficient-in-emitting-light-2718190.html
2014.09.07 View 11640 -
Discovery of New Therapeutic Targets for Alzheimer's Disease
A Korean research team headed by Professor Dae-Soo Kim of Biological Sciences at KAIST and Dr. Chang-Jun Lee from the Korea Institute of Science and Technology (KIST) successfully identified that reactive astrocytes, commonly observed in brains affected by Alzheimer’s disease, produce abnormal amounts of inhibitory neurotransmitter gamma-Aminobutyric acid (GABA) in reaction to the enzyme Monoamine oxidase B (Mao-B) and release GABA through the Bestrophin-1 channel to suppress the normal signal transmission of brain nerve cells.
By suppressing the GABA production or release from reactive astrocytes, the research team was able to restore the model mice's memory and learning impairment caused by Alzheimer’s disease. This discovery will allow the development of new drugs to treat Alzheimer’s and other related diseases.
The research result was published in the June 29, 2014 edition of Nature Medicine (Title: GABA from Reactive Astrocytes Impairs Memory in Mouse Models of Alzheimer’s Disease).
For details, please read the article below:
Technology News, July 10, 2014
"Discovery of New Drug Targets for Memory Impairment in Alzheimer’s Disease"
http://technews.tmcnet.com/news/2014/07/10/7917811.htm
2014.07.16 View 8336 -
Artificial Antibody-based Therapeutic Candidate for Lung Cancer Developed
Professor Hak-Sung Kim of Biological Sciences at KAIST publishes a cover article on artificial antibody in "Molecular Therapy".
Repebody-based lung cancer therapeutic drug candidate developed Repebody-based protein demonstrates the possibility of the development of a new drug
KAIST Biological Sciences Department’s Professor Hak-Sung Kim, in collaboration with Professor Eun-Kyung Cho from the College of Medicine at Chungnam National University, has successfully developed an artificial antibody-based, or repebody, cancer therapeutic candidate. These research results were published as a cover paper of the July edition of Molecular Therapy.
The repebody developed by Professor Kim and his team strongly binds to interleukin-6, a cancer-causing factor. It has also been confirmed that the repebody can significantly inhibit the proliferation of cancer cells in non-small-cell lung cancer animal model.
Numerous multinational pharmaceutical and biotechnology companies have invested astronomical amounts of money in research for the development of protein therapeutics with low side effects and high efficacy. More than 20 kinds of such therapeutics are currently under clinical trials, and over 100 drugs are under clinical demonstration. Among these, the majority is antibody-based therapeutics, and most of the investments are heavily concentrated in this field. However, antibody production cost is very high because it has large molecular weights and complex structural properties, and this makes it difficult to engineer. Consequently, the development costs a great deal of time and money.
In order to overcome the existing limitations of antibody-based therapeutics, Professor Kim and his team have developed a new artificial antibody, or repebody, which was published in Proceedings of the National Academy of Sciences (PNAS) in 2012. Based on this research, they have succeeded in developing a therapeutic candidate for treating non-small-cell lung cancer with a specifically strong cohesion to the cancer-causing factor, interleukin-6.
Interleukin-6 is a crucial substance within the body that is involved in immune and inflammatory-related signals. When abnormally expressed, it activates various carcinogenic pathways and promotes tumor growth and metastasis. Because of its importance, multinational pharmaceutical companies are heavily investing in developing therapeutics that can inhibit the signaling of interleukin-6.
In this study, Professor Kim and his team observed that a repebody consists of repeated modules, and they conceived a module-based affinity amplification technology that can effectively increase the binding affinity with the disease target. The developed therapeutic candidate has been confirmed in cell and animal experiments to show low immunogenicity, as well as to strongly inhibit the proliferation of non-small-cell lung cancer.
Furthermore, by investigating the complex structure of the repebody with interleukin-6, Professor Kim has identified its mechanism, which demonstrated the potential for therapeutic development. The researchers are currently carrying out pre-clinical trials for acquiring permission to perform clinical trials on animals with non-small-cell lung cancer. The repebody can be developed into a new protein drug after demonstrating its safety and efficacy.
Professor Hak-Sung Kim and his team have confirmed that the repebody can be utilized as a new protein drug, and this will be a significant contribution to Korea’s protein drugs and biotechnology industry development.
The research was supported by the Future Pioneer Industry project and sponsored by the Ministry of Science, ICT and Future Planning.
Figure 1. Professor Kim’s article published as the cover article of July edition of Molecular Therapy
Figure 2. Clinical proof of the repebody’s inhibition of cancer growth using animal models
2014.07.14 View 12081 -
2014 Conference on Korean Sociology Held at KAIST
The Korean Sociological Association (KSA) hosted a two-day conference in 2014 entitled “In the age of anxiety, sociology can present answers” at the College of Liberal Arts and Convergence Science, KAIST, on June 20-21, 2014. Professor Jung-Ro Yoon of the Department of Humanities and Social Sciences at KAIST is the President of KSA. The conference addressed issues such as big data and risk society. During the conference, 40 sessions took place, and 150 research papers were released.
Professor Yoon said, “The conference will offer a great opportunity for Korean sociologists to discuss anxiety, chaos, risk, and the uncertainty that Korean society experiences and suggest answers and a new vision upon which Korean society should move forward.”
2014.06.22 View 7462 -
Professor Won Do Heo on LED Light Technology for Controlling Proteins in Living Cells
With the newly developed LED technology, Professor Won Do Heo at the College of Life Science and Bioengineering, KAIST, was able to suppress cell migration and division when cells are exposed to LED light. This suggests a breakthrough to apply in future cancer cell research.
Professor Heo talked about the impact of his research in the following excerpt from a news article:
“We are already conducting research on the spread of cancer, as well as brain science in animal models with the Light-Activated Reversible Inhibition by Assembled Trap. I believe this technology will be a breakthrough in investigating cancer treatments and the function of neurons in a complex neural network, which existing technologies have not been able to do.”
From EE Times Europe, June 19, 2014
“LED Light Technology Controls Proteins in Living Cells”
http://www.ledlighting-eetimes.com/en/led-light-technology-controls-proteins-in-living-cells.html?cmp_id=7&news_id=222909336
2014.06.22 View 7530 -
Binding Regulatory Mechanism of Protein Biomolecules Revealed
Professor Hak-Sung Kim
A research team led by Professor Hak-Sung Kim of Biological Sciences, KAIST, and Dr. Mun-Hyeong Seo, KAIST, has revealed a regulatory mechanism that controls the binding affinity of protein’s biomolecules, which is crucial for the protein to recognize molecules and carry out functions within the body.
The research results were published in the April 24th online edition of Nature Communications.
The protein, represented by enzyme, antibody, or hormones, specifically recognizes a variety of biomolecules in all organisms and implements signaling or immune response to precisely adjust and maintain important biological processes. The protein binding affinity of biomolecules plays a crucial role in determining the duration of the bond between two molecules, and hence to determine and control the in-vivo function of proteins.
The researchers have noted that, during the process of proteins’ recognizing biomolecules, the protein binding affinity of biomolecules is closely linked not only to the size of non-covalent interaction between two molecules, but also to the unique kinetic properties of proteins.
To identify the basic mechanism that determines the protein binding affinity of biomolecules, Professor Kim and his research team have made mutation in the allosteric site of protein to create a variety of mutant proteins with the same chemical binding surface, but with the binding affinity vastly differing from 10 to 100 times. The allosteric site of the protein refers to a region which does not directly bind with biomolecules, but crucially influences the biomolecule recognition site.
Using real-time analysis at the single-molecule level of unique kinetic properties of the produced mutant proteins, the researchers were able to identify that the protein binding affinity of biomolecules is directly associated with the protein’s specific kinetic characteristics, its structure opening rate.
Also, by proving that unique characteristics of the protein can be changed at the allosteric site, instead of protein’s direct binding site with biomolecules, the researchers have demonstrated a new methodology of regulating the in-vivo function of proteins.
The researchers expect that these results will contribute greatly to a deeper understanding of protein’s nature that governs various life phenomena and help evaluate the proof of interpreting protein binding affinity of biomolecules from the perspective of protein kinetics.
Professor Kim said, “Until now, the protein binding affinity of biomolecules was determined by a direct interaction between two molecules. Our research has identified an important fact that the structure opening rate of proteins also plays a crucial role in determining their binding affinity.”
[Picture]
A correlation graph of opening rate (kopening) and binding affinity (kd) between protein’s stable, open state and its unstable, partially closed state.
2014.05.02 View 9305 -
Extreme Tech: Nanowire "impossible to replicate" fingerprints could eliminate fraud, counterfeit goods
Research done by Professor Hyun-Joon Song of Chemistry at KAIST on
anti-counterfeit, nanoscale fingerprints generated by randomly distributed
nanowires was introduced by Extreme Tech, an online global science and technology
news.
For the articles, please go to:
Extreme Tech, March 25, 2014Nanowire ‘impossible to replicate’ fingerprints could eliminate fraud, counterfeit goods
http://www.extremetech.com/extreme/179131-nanowire-impossible-to-replicate-fingerprints-could-eliminate-fraud-counterfeit-goods
2014.03.26 View 7781 -
KAIST Holds Open Lecture For Daejeon Residents
Free of cost for any Korean citizen, the registration for the new course opens on the official website from 5th March KAIST’s Department of Humanities and Social Science is currently operating free humanities and liberal arts classes for Daejeon residents.
The theme of the course for this semester is “World and Politics,” which will begin on 13th March and run every Thursday for 6 weeks at KAIST’s International Seminar Room.
This course has been organized to introduce the general public to the current political situation with neighboring countries such as China, Japan and North Korea, as well as the characteristics of multinational companies.
Top experts in the related fields will give lectures. First, Professor Ha-Yong Jung from Kyunghee University will talk on “American liberalism and democracy”; Professor Gyeong-Mo An from Korea National Defense University on “Kim Jeong-Eun and the Future of North Korea--Is the Collapse of North Korea A Reality?” and Ja-Seon Koo, a visiting professor at Korea National Diplomatic Academy on “The Chinese Communist Party during the Xi Jinping Period.”
“With the era of globalization, the political situations in the neighboring countries have both direct and indirect effects on our lives,” said Professor Hyeon-Seok Park who has organized the courses. "These classes will be an opportunity for our citizens to understand and learn about the current affairs in the world.”
Anyone can attend the course, and registration is from March 5th to 9th at the official webpage of KAIST’s Humanities and Social Sciences Department (http://hss.kaist.ac.kr). All the courses are free of charge.
Contact: Department of Humanities and Social Science Research (Tel. 350-4687, E-mail: baobab@kaist.ac.kr)
2014.03.06 View 6382 -
Professor Suk-Bok Chang receives 14th Korea Science Award in the field of Chemistry
Professor Suk-Bok Chang from the Department of Chemistry at KAIST received the “2013 Korea Science Award” in chemistry hosted by the National Research Foundation and the Ministry of Science, ICT, and Future Planning, Republic of Korea.
The Korea Science Award is a presidential award of Korea, which was first established in 1987 to recognize research excellence in natural science. Three scientists are selected for the award in every other year.
Professor Chang primarily researches the catalyzing mechanism of carbon-hydrogen bonds in organic molecules. He has succeeded in making great progress in the field of organic chemistry especially in developing a new type of transition metal catalytic behavior that can be applied to low-reactivity compounds.
Hydrocarbons are abundant in nature, but its unreactive nature in ambient conditions makes it unsuitable as reactant for compound synthesis. In addition, the mechanism behind transition metal catalyzed carbon-hydrogen bond synthesis has not been proven sufficiently.
The prediction that fossil fuels will be depleted before the end of the century makes hydrocarbon synthesis an extremely important matter.
The need for an effective hydrocarbon synthesis method inspired Professor Chang to pursue research in the transition metal catalysis method and to develop a catalytic system that would allow efficient synthesis even in ambient conditions.
Professor Chang has been the lead researcher for the Institute for Basic Science’s “molecule catalysis reaction research team” since December 2012 and has been carrying out this research in KAIST.
2014.01.27 View 9519 -
Mechanism in regulation of cancer-related key enzyme, ATM, for DNA damage and repair revealed
Professor Kwang-Wook Choi
A research team led by Professor Kwang-Wook Choi and Dr. Seong-Tae Hong from the Department of Biological Sciences at KAIST has successfully investigated the operational mechanism of the protein Ataxia Telangiectasia Mutated (ATM), an essential protein to the function of a crucial key enzyme that repairs the damaged DNA which stores biometric information. The results were published on December 19th Nature Communications online edition.
All organisms, including humans, constantly strive to protect the information within their DNA from damages posed by a number of factors, such as carbonized materials in our daily food intake, radioactive materials such as radon emitting from the cement of buildings or ultraviolet of the sunlight, which could be a trigger for cancer.
In order to keep the DNA information safe, the organisms are always carrying out complex and sophisticated DNA repair work, which involves the crucial DNA damage repair protein ATM. Consequently, a faulty ATM leads to higher risks of cancer.
Until now, academia predicted that the Translationally Controlled Tumor Protein (TCTP) will play an important role in regulating the function of ATM. However, since most of main research regarding TCTP has only been conducted in cultured cells, it was unable to identify exactly what mechanisms TCTP employs to control ATM.
The KAIST research team identified that TCTP can combine with ATM or increase the enzymatic activity of ATM. In addition, Drosophilia, one of the most widely used model organisms for molecular genetics, has been used to identify that TCTP and ATM play a very important role in repairing the DNA damaged by radiation. This information has allowed the researchers to establish TCTP’s essential function in maintaining the DNA information in cell cultures and even in higher organisms, and to provide specific and important clues to the regulation of ATM by TCTP.
Professor Kwang-Wook Choi said, “Our research is a good example that basic research using Drosophilia can make important contributions to understanding the process of diseases, such as cancer, and to developing adequate treatment.”
The research has been funded by the Ministry of Science, ICT and Future Planning, Republic of Korea, and the National Research Foundation of Korea.
Figure 1. When the amount of TCTP protein is reduced, cells of the Drosophila's eye are abnormally deformed by radiation. Scale bars = 200mm
Figure 2. When the amount of TCTP protein is reduced, the chromosomes of Drosophilia are easily broken by radiation. Scale bars = 10 mm.
Figure 3. When gene expressions of TCTP and ATM are reduced, large defects occur in the normal development of the eye. (Left: normal Drosophilia's eye, right: development-deficient eye)
Figure 4. ATM marks the position of the broken DNA, with TCTP helping to facilitate this reaction. DNA (blue line) within the cell nucleus is coiled around the histone protein (green cylinder). When DNA is broken, ATM protein attaches a phosphate group (P). Multiple DNA repair protein recognizes the phosphate as a signal that requires repair and gathers at the site.
2014.01.07 View 11790