| 為了能夠使我們更有效地拿到我們的指定抗菌肽，我們在設計序列時在AMPs的N-terminal加上了來自S.lividans幾丁質酶C的signal peptide (附上氨基酸序列)。這個pre-mature peptide在經過periplasmic space時會被peptidase辨認並且做切割。Peptidase會辨認signal peptide 上Ala-Gln-Ala序列，並且從signal和mature peptide中間的兩個Ala間將之分開。為了使peptidase能夠順利辨認並且切割，我們在AMP的N-terminal多加了一個Ala氨基酸，以確保整個系統能順利運作。
我們利用模擬技術，利用原本的已知結構，去推測在我們多加了一個Ala的情況下，是否會影響AMPs的蛋白結構折疊。
In order to have more efficient to get our AMPs, we treated signal peptide upstream of the N-terminal of mature antimicrobial peptides. This signal peptide is comes from chitinase C of S.lividans (MGFRHKAAALAATLALPLAGLVGLASPAQA). When the pre-mature peptides go through the periplasmic space, peptidase will identified the cleavage site Ala-Gln-Ala and cut at the double Ala between the signal and mature peptide.
To make sure the secretion system is work we attach an Ala at the N-terminal of AMPs. We used protein secondary structure prediction software base on the known peptide structure to analysis whether the attached Ala affect the peptide folding process or not.
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