투고논문
| JKRMS Volume 28, No 4, pp 44, Backbone NMR assignments of reco... | |
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| 2024년 12월 20일 / 조회수: 211 | |
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Backbone NMR assignments of recombinant glucagon at pH 6.0 Sung-Hee Lee1,2,§, Seong-Eun Park1,3,§, Kyeong-Hyeon Yoon1,3, Young-Ho Lee4-8, Eun-Hee Kim4, Hae-Kap Cheong4, Ji-Hun Kim2 and Hyung-Sik Won1,3,* 1Department of Biotechnology and Research Institute for Biomedical & Health Science, College of Biomedical & Health Science, Konkuk University, Chungju, Chungbuk 27478, Republic of Korea 2College of Pharmacy, Chungbuk National University, Cheongju, Chungbuk 28160, Republic of Korea 3BK21 Project Team, Department of Applied Life Science, Graduate School, Konkuk University, Chungju, Chungbuk 27478, Republic of Korea 4Biopharmaceutical Research Center, Korea Basic Science Institute, Cheongju, Chungbuk 28119, Republic of Korea 5Bio-Analytical Science, University of Science and Technology, Daejeon 34113, Republic of Korea 6Graduate School of Analytical Science and Technology, Chungnam National University, Daejeon 34134, Republic of Korea 7Department of Systems Biotechnology, Chung-Ang University, Gyeonggi 17546, Republic of Korea 8Frontier Research Institute for Interdisciplinary Sciences, Tohoku University, Sendai, Miyagi 980-8578, Japan Received Nov 25, 2024; Revised Dec 2, 2024; Accepted Dec 3, 2024 Abstract The peptide hormone glucagon has served as both a biopharmaceutical agent for clinical use and a model peptide forming amyloid fibrils. As we recently established a recombinant production of glucagon, its backbone NMR assignments at neutral pHs were conducted in the present study. However, as the NMR spectra showed severe line broadening and poor dispersion at pHs 7.5 and 7.0, complete backbone NMR assignments could be obtained at pH 6.0. Interestingly, CSI and TALOS predictions using the assigned chemical shift values indicated different probabilities of secondary structure. These results suggest that glucagon would adopt an unusual or dynamically fluctuating conformation in solution. Therefore, detailed conformation and molecular dynamics of glucagon would be worthy of investigation, for which the present results provide an experimental basis. Keywords amyloid fibril, backbone NMR assignments, glucagon, secondary structure *Address correspondence to: Hyung-Sik Won, Department of Biotechnology, Konkuk University, Chungju, Chungbuk 27478, Korea Tel: 82-43-840-3589; E-mail: wonhs@kku.ac.kr § These authors contributed equally to this work. |
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| 첨부파일 | 3. JKMRS_WonHS_pp44-50.pdf |