Study on Conformation Transitions of Trichokonin Ⅵ, a Peptaibol-Like Antimicrobial Peptide, in Different Solvents by Circular Dichroism Spectroscopy
DONG Xiao-wei1, 4, SONG Xiao-yan2, 3*, SHI Mei2, ZHANG Yu-zhong2
1. School of Life Sciences, Shandong Normal University, Ji’nan 250114, China 2. State Key Laboratory of Microbial Technology, Shandong University, Ji’nan 250100, China 3. School of Medical and Life Science, Jinan University, Ji’nan 250223, China 4. Technology Center, Shandong Tobacco Industry Corporation, Ji’nan 250013, China
Abstract：Trichokonin Ⅵ, a peptaibol-like antimicrobial peptides isolated from the cultured substrates of trichoderma koningii SMF2, has 20 amino acid residues. The conformational flexibility of trichokonin Ⅵ in organic solvents with different polarities, aqueous solvents and membrane mimic solvents was studied by circular dichroism spectroscopy. Trichokonin Ⅵ takes on a typical α-helical structure in different organic solvents, but helicity decreases in aqueous solvent. The helical content increases with increasing the concentration of TFE up to 30%. In phosphate buffered saline, the CD spectrum of trichokonin Ⅵ is concentration dependent, and the intensity of the peaks increases with increasing the concentration of trichokonin Ⅵ. SDS induces a significant transition towards a helix formation, and the CD spectra in membrane mimic solvents increase helicity compared with those recorded without membrane mimic solvents, suggesting the interaction of the peptides with the membrane.
董小卫1, 4，宋晓妍2，3*，石 梅2，张玉忠2 . Peptaibols类抗菌肽—Trichokonin Ⅵ在不同溶剂中构象变化的圆二色谱研究[J]. 光谱学与光谱分析, 2010, 30(02): 458-461.
DONG Xiao-wei1, 4, SONG Xiao-yan2, 3*, SHI Mei2, ZHANG Yu-zhong2 . Study on Conformation Transitions of Trichokonin Ⅵ, a Peptaibol-Like Antimicrobial Peptide, in Different Solvents by Circular Dichroism Spectroscopy. SPECTROSCOPY AND SPECTRAL ANALYSIS, 2010, 30(02): 458-461.
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