Loss of second and sixth conserved cysteine residues from trypsin inhibitor-like cysteine-rich domain-type protease inhibitors in Bombyx mori may induce activity against microbial proteases

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• 作者：Youshan Li^a ; ^b ; Huawei Liu^a ; Rui Zhu^c ; Qingyou Xia^a ; Ping Zhao^a ; ^{zhaop@swu.edu.cn}
• 关键词：TIL ; trypsin inhibitor-like cysteine-rich domain ; p28 ; a derivative expression plasmid of pET28a ; NTA ; nitrilotriacetic acid ; CD ; circular dichroism ; MALDI-TOF/TOF MS ; matrix-assisted laser desorption/ionization time-of-flight/time-of-flight mass spectrometry ; FITC-Casein ; fluoresceinisothiocyanate-casein
• 刊名：Peptides
• 出版年：2016
• 出版时间：December 2016
• 年：2016
• 卷：86
• 期：Complete
• 页码：13-23
• 全文大小：2641 K
• 卷排序：86

文摘

The Cys2nd and Cys6th were missing from silkworm TIL-type protease inhibitors. Introduction of Cys2nd and Cys6th may cause incorrect disulfide bond formation. Cysteine mutations caused a slight change in the secondary structure composition. Cysteine mutations affected the multimerization states of protease inhibitors. Cys2nd and Cys6th mutations dramaticly reduced the activity of protease inhibitors.