Abstract
In the past decades, a great amount of antimicrobial peptides (AMPs) has been discovered, the structure identification of which relies heavily on de novo sequencing by Edman degradation or mass spectrometry. Here we outline the basic procedures for the exact mass measurement approaches that use off-line low-energy CID ESI Qq-TOF MS/MS in positive-ion mode, which is typically applied to de novo sequencing of peptides, to elucidate the structure of AMPs. Ambiguity I/L and partial sequence order were elucidated by Edman degradation or/and structural similarity analysis to known sequence. The approaches can determine the structure of peptides composed of as much as 38 amino acids in our practice.
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Acknowledgment
We thank Zhijun Wu and Feng Xie. This work was supported by the National Natural Science Foundation of China (30800100), the Chinese Academy of Sciences (CIB-2007-LYQY-01), the Science and Technology Office of Guiyang (2012204), and the Science and Technology Department of Sichuan (2008JY0001).
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Liu, J., Jiang, J. (2017). Mass Spectrometry Approaches for Determining the Structure of Antimicrobial Peptides. In: Hansen, P. (eds) Antimicrobial Peptides. Methods in Molecular Biology, vol 1548. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6737-7_7
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DOI: https://doi.org/10.1007/978-1-4939-6737-7_7
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