Secret of Peptoid 3 Dimension Structure Control Unveiled
- Professor Seo Ji-won, Yun Myung-han, student researcher, Shin Hye-min posted research paper in Chemical Communications
- Helical structure changes by position and number of monomer…Kang Chang-mook, a student at GIST participated as a second author

 

 

 

□ Research team including an undergraduate student of GIST(Gwangju Institute of Science and Technology, President  Young Joon Kim) unveiled the mechanism of controlling 3 dimension structure of peptoid*, synthetic cousins of protein in helical shape developed to imitate function of bio protein. The peptoid 3 dimension structure control mechanism is expected to be widely used in various fields including artificial photosynthetic materials, allowing precision control of synthetic protein with various functionalities.

* Peptoid is new substance developed to generate synthetic protein. It is a derivant of peptide, biopolymer formed with less than 40 amino acid and is widely used to design synthetic protein as it is easy to build a 2^nd structure including helical structure.

□ Led by professor Seo Ji-won at Division of Liberal Arts and Sciences at GIST College and professor Yun Myung-han (co-corresponding author) at School of Material Science & Engineering and performed by Shin Hye-min, a student researcher of School of Material Science & Engineering (fist author in PhD program) and Kang Chang-mook (second author, a senior at  GIST College), the research was conducted with the support of general researcher support project of National Research Foundation of Korea and support from solar cell technology development and research foundation building project of Research Institute for Solar and Sustainable Energies of GIST and the result was posted on line in the March 7^th edition of Chemical Communications, a renowned scientific journal of chemistry.

* Paper title: Peptoid helicity modulation: precise control of peptoid secondary structures via position-specific placement of chiral monomers.)

□ Living things require numerous bio mechanisms and functionalities including creation and storage of optical energy and defense mechanism to fight for the body system and bio protein is the key molecule to enable these functionalities.

o Since bio protein is optimized to function inside body system, once it gets out of the system, it is difficult to ensure stable functionality. Thus, research on bioinspired synthetic protein is actively performed to find a way to use it as materials for various purposes outside of body system.

o Peptoid is the derivant of peptide* and one of the most popular research subject in synthetic protein research. It has similar sequence with peptide but is more stable as it is built in synthetic structure and since precise control is possible, it is widely used as materials for protein biomimetics. Control over the 3 dimension structure of peptoid is critical for practical and diversified research as it allows building flexible formation with peptoid.

□ GIST research team discovered modifying the location and number of monomer* in the sequential chain, the key to build peptoid structure, enables precise control over helical structure and folding.

o Using circular Dichroism spectroscopy, the research team discovered the second position of N-terminus and the first position of C-termins are the key to peptoid formation and changing the types of monomers on these locations can modify helical structure of peptoid.

□ The research findings enable flexible programming and more precise control over helical structure of synthetic protein and diverse applications across various fields of biomimetics artificial photosynthetic material development and smart biological response modifier design.

□ Professor Seo Ji-won said “The research findings can be a breakthrough in synthetic protein design imitating the optimal system of bio protein. It is expected to contribute to a wider spectrum of research areas including energy materials and medicine with application to artificial photosynthesis and anti biotic peptide.”