人抗菌肽FALL-39突变分子的特性和抗菌功能的比较

Comparing the protein characteristics and antibacterial activity of antibacterial peptide FALL-39 and its mutant peptides

目的对人抗菌肽FALL-39不同突变分子蛋白的特性及抗菌功能进行初步的比较。方法应用AU-PAGE电泳、RP-HPLC、Om iga蛋白分析软件,比较FALL-39及其突变蛋白FALL-39-Lys24、FALL-39-Lys32、FALL-39-Lys24′32的特性;测定M IC、MEC和MBC值,并比较抗菌作用。结果突变蛋白AU-PAGE电泳迁移速率较快,RP-HPLC出峰时间未见改变,蛋白的亲疏水性、α螺旋结构、抗原性等蛋白特性无明显改变。M IC、MEC和MBC值表明FALL-39突变肽对大肠杆菌和绿脓杆菌的抗菌活性有所增强。结论突变蛋白在增加正电荷的同时,虽未改变蛋白的特性,但抗菌活性增强。

OBJECTIVE To compare the protein characteristics of antibacterial peptide FALL- 39 and its mutant peptides. METHODS Using AU - PAGE elution, HPLC and omiga analysis software, the protein characteristics of purified peptides of FALL - 39 and its mutant peptides, FALL-39- Lys32, FALL- 39 -Lys24 and FALL- 39 -Lys24＇32 were analyzed. MEC, MIC and MBC were used to assay the antibacterial activities of these peptides. The antibacterial assay showed that mutant peptides were more potent in the antibacterial activity against E. coli ATCC 25922, E. coli ML 35p and Pseudomonas aeruginosa ATCC 27853 than that of FALL - 39. RESULTS FALL - 39 mutants peptides ran faster than FALL - 39 in AU- PAGE elution, while the retention time of HPLC. Hydrophobicity, protein flexibility and yon heijne transmembrane helices did not change. CONCLUSION FALL - 39 mutant peptides have increasing antibacterial activity and net positive charge, but with no protein characteristics change.