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Cecropin Cecropins are antimicrobial peptides. They were first isolated from the hemolymph of ''Hyalophora cecropia'', whence the term cecropin was derived. Cecropins lyse bacterial cell membranes; they also inhibit proline uptake and cause leaky membranes. Cecropins constitute a main part of the cell-free immunity of insects. Cecropins are small proteins of about 31 - 37 amino acid residues active against both Gram-positive and Gram-negative bacteria. Cecropins isolated from insects other than ''Hyalophora cecropia'' (Cecropia moth) have been given various names; bactericidin, lepidopteran, sarcotoxin, etc. All of these peptides are structurally related. Cecropin P1, an intestinal antibacterial peptide from ''Sus scrofa'' (Pig), also belongs to this family. Cecropin family also consists Cecropin A and Cecropin B. Cecropin is an anticancer polypeptide(L). Structure consists of mainly alpha helixes, determined by solution NMR. Protein molecular weight = 4203.4g/mol.〔 〕 At low peptide to lipid ratios ion channels are formed, at high peptide to lipid ratios pores are formed.〔Loraine Susan Silvestro, "Function and structure of cecropin A" (January 1, 2000). Dissertations available from ProQuest. Paper AAI9965567. http://repository.upenn.edu/dissertations/AAI9965567〕 ==References==
抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)』 ■ウィキペディアで「Cecropin」の詳細全文を読む
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