抗癌肽改造及其对人乳腺癌MCF7作用的评估  

Transformation of anticancer peptides and the evaluation of their anticancer activities against MCF7 human breast cancer cells

作　　者：党军龙[1] 周礼红[2] DANG Jun-long ZHOU Li-hong(School of Pharmaceutical Science, Guizhou University, Guiyang, Guizhou 550025, China Institute of Fungus Resources, College of Life Science, Guizhou University, Guiyang, Guizhou 550025, China)

机构地区：[1]贵州大学药学院,贵州贵阳550001 [2]贵州大学生命科学学院真菌资源研究所,贵州贵阳550001

出　　处：《山地农业生物学报》2016年第4期72-76,共5页Journal of Mountain Agriculture and Biology

基　　金："十二五"农村领域国家科技计划课题子课题(2012BAD33B06)

摘　　要：为了探讨不同净电荷及疏水度对天然多肽CMAP-8衍生物抗人乳腺癌细胞MCF7增殖抑制作用的影响,分别采用带正电荷的K和疏水性的F两种氨基酸对天然多肽CMAP-8进行设计改造,得到系列衍生物。其净电荷数为0~8,疏水度为42%~57%,采用MTT法检测所得多肽衍生物对人乳腺癌细胞MCF7的增殖抑制率,Anti CP对多肽抗癌活性的预测。结果表明,净电荷为0的多肽均没有预测抗肿瘤活性,可能是因为多肽的净电荷对其预测活性有一定的影响。体外抗乳腺活性结果表明,CMAP-L-20、CMAP-L-23、CMAP-L-24和CMAP-L-25对MCF7细胞的抑制率与CMAP-8相比,差异达到了极显著水平（Duncan-test,P〈0.01）。所筛选的4条多肽净电荷数为6~8,疏水度均为46%,而天然多肽CMAP-8净电荷为0,疏水度为42%。多肽活性预测结果与体外抗乳腺癌检测结果一致,共同表明了净电荷的改变对多肽抗乳腺癌活性的影响更大,而疏水度并非越大越好,应该处在合适的范围内。Positive charged lysine and hydrophobic phenylalanine were employed to transform the naturally occurred peptide CMAP-8 in order to explore the effects of net charge and hydrophobicity on anticancer activity of anticancer peptides（ ACPs） against MCF7 human breast cancer cells. A sequence of derived peptides was transformed,with the net charge and hydrophobicity ranged from 0 to 8 and 42% to 57%,respectively. The anticancer activities of the peptides predicted by Anti CP demonstrated that all the peptides without net charge did not show predicted anti-tumor activities. The proliferating inhibitory effects results indicated that the inhibitory effects of peptides CMAP-L-20、CMAP-L-23、CMAP-L-24 and CMAP-L-25 on MCF7 were highly significant（ Duncan-test,P0.01）,compared with natural CMAP-8. The effect may attribute to the net charge of the peptides affecting the anticancer activities. The net charges of the four screened derived peptides（ CMAP-L-20、CMAP-L-23、CMAP-L-24 and CMAP-L-25） ranged from 6 to 8,and their hydrophobicity were all at46%,compared with the net charge and hydrophobicity of the natural peptide CMAP- 8 of 0 and 42%,respectively. The predicted anticancer activities of the peptides were consistent with the in vitro test results,which indicated that the netcharge of ACPs plays a more significant role in their anti-tumor activities against breast carcinoma cells. However,the higher hydrophobicity is not necessary better and it should be in an appropriate range rather than be much higher.

关 键 词：净电荷 CMAP-8 乳腺癌 抑制作用 

分 类 号：R979.19[医药卫生—药品]