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| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Grand Ballroom |
| Time |
10월 19일 (금요일) 11:00~12:30 |
| Code |
LIFE.P-413 |
| Subject |
Biochemical Characterization and Structural Studies of engineered novel antimicrobial peptides |
| Authors |
Ji Sun Kim , Ji-Ho Jeong, Yongae Kim*
Department of Chemistry, Hankuk University of Foreign Studies, Korea
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| Abstract |
Since the discovery of penicillin, antibiotics have brought benefits such as prolonging human life, treating bacterial infections as well as promoting animal growth, but misuse and abuse of antibiotics have caused serious public health problems and economic losses. In addition, unnecessary prescriptions have caused many side effects, and the most problematic is the emergence of super bacteria with antibiotic resistance. Furthermore, due to the scientific difficulties of development and the rapid emergence of antibiotic-resistant bacteria, new types of antibiotics have not been developed in the past 30 years, and therefore the spread of super bacteria resistant to antibiotics is a matter of time. Thus, antibiotics that work in a completely different way from conventional antibiotics have become necessary, and long-term solutions to these problems include antimicrobial peptides produced by all organisms, from bacteria to vertebrates and invertebrates.
We have successfully identified the structure and activity of Lactophoricin (LPcin), an antimicrobial peptide found in bovine milk, through expression using recombinant DNA technology, purification using various biophysical techniques, and structural studies using liquid/solid-state NMR. Based on this, we constructed a total of 20 analogs library through conservative sequence modification to develop new antimicrobial peptides with shorter length and improved antimicrobial activity than conventional LPcin. Among them, six new antimicrobial peptides were selected through bacterial killing assays and growth inhibition assays, and each peptide was obtained a high purity, sufficient amount for structural studies by optimization of the expression and purification process. In addition, each peptide identified its potential as a new antibiotic through hemolysis assay and cytotoxicity assay, and to investigate the relationship between active-structure by conducting a 3D topology structure study using liquid/solid-state NMR.
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| E-mail |
cucu860@daum.net |
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122nd General Meeting of the KCS