牛乳铁蛋白活性肽（LactoferricinB）（3—17）与蜂毒肽（Melittins）（6—12）杂合多肽活性功能的测定

Determination of the Heterozygous Peptide Activity of Lactoferricin B（ 3-17 ）and Melittins （ 6-12 ）

抗菌肽近年逐渐成为研究的热点。将牛乳铁蛋白活性多肽（LfcinB）与蜂毒肽（Melittins）核心功能区间，即LfcinB的3-17位的15个氨基酸与Melitins的6-12位的8个氨基酸，固相合成新的多肽分子Lfb15-Me8。经RT-HPLC和质谱检测合成多肽分子准确，纯度达到98％以上。经体外抑菌实验证明，所合成的新型抗菌肽分子对大肠杆菌ATCC25922、金黄色葡萄球菌ATCC25923、绿脓杆菌ATCC27853、酵母GS115、沙门氏菌ATCC12291的最小抑菌浓度（MIC）分别为16μg·mL^-1、32μg·mE-164μg·mL^-1、128μg·mL^-1、16μg·mL^-1，并在其抗菌浓度下并未表现溶血特性。获得了具有活性的新型多肽序列，为抗菌肽的研发奠定了新的研究内容。

In recent years, antibacterial peptides have become a research focus. This research conducted solid-phase synthesis on core function range of the bovine lactoferrin peptide （Lfcin B） and melittin （Melitins）, 15 amino acids of 3-17 bit Lfcin B and 8 amino acids of 6-12 bit Melitins, into new polypeptide molecule Lfbl5-Me8. The peptide molecules were accurate after detection and synthesis of RT-HPLC and mass spectrometry and purity reached more than 98%. The vitro experiments proved that the minimum inhibitory concentration （MIC） of synthesized new peptide molecules against E.coli ATCC25922, Staphylococcus aureus ATCC25923, Pseudornonas aeruginosa ATCC27853, yeast GS115, Sdmonella ATCC12291 were 16μg·mL^-1、32μg·mE-164μg·mL^-1、128μg·mL^-1、16μg·mL^-1 respectively, and its antimicrobial concentration did not show hemolytic properties. The new active peptide sequence was obtained and new research content has been laid for peptide research ＆ development.