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Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
Published on: April 14, 2015
Extensive characterization and differential analysis of endogenous peptides from Bombyx batryticatus using mass
Yunpeng Bai1, Qiang Zhao2, Meixi He2
1CAS Key Laboratory of Separation Sciences for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Zhongshan Road 457, Dalian 116023, China.
Abstract:
Bombyx batryticatus, the dried larva of Bombyx mori L. (4th-5th instars) infected with Beauveria bassiana Vuill, is an important animal-derived medicine effective against several diseases. The metamorphosis of silkworm can result insignificant changes in the levels of proteins and polypeptides in the 4th and 5th instar larvae. Here, we performed extensive characterization of Bombyx batryticatus peptides, including polypeptides containing cysteines, using an MS-based data mining strategy. A total of 779 peptides with various PTMs (post-translational modifications) were identified through database search and de novo sequencing. Some of these peptides might have important biological activities. Besides, the differential analysis of polypeptides between the head and body of Bombyx batryticatus was performed to provide a clinical basis for rational use of the drugs derived from it. This study illustrates the abundance and sequences of endogenous Bombyx batryticatus polypeptides, and thus, provides potential candidates for the screening of active compounds for future biological research and drug discovery studies.
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