Odell E W, Sarra R, Foxworthy M, Chapple D S, Evans R W
Department of Oral Medicine and Pathology, UMDS Guy's Hospital Dental School, London, U.K.
FEBS Lett. 1996 Mar 11;382(1-2):175-8. doi: 10.1016/0014-5793(96)00168-8.
Human lactoferrin contains a 46 residue sequence named lactoferricin H thought to be responsible for its antimicrobial properties. Synthetic peptides HLT1, corresponding to the loop region of human lactoferricin (FQWQR-NMRKVRGPPVS) and HLT2, corresponding to its charged portion (FQWQRNMRKVR), exerted significant antibacterial effects against E. coli serotype O111 strains NCTC 8007 and ML35. The corresponding sequences in native human lactoferrin were shown to adopt a charged helix and hydrophobic tail within the N-lobe remote from the iron binding site. Sequence similarities between lactoferricin and dermaseptin and magainins suggest that lactoferricin may act as an amphipathic alpha helix.
人乳铁蛋白包含一段46个残基的序列,称为乳铁杀菌肽H,被认为与其抗菌特性有关。合成肽HLT1对应于人乳铁杀菌肽的环区域(FQWQR-NMRKVRGPPVS),HLT2对应于其带电部分(FQWQRNMRKVR),对大肠杆菌O111血清型菌株NCTC 8007和ML35具有显著的抗菌作用。天然人乳铁蛋白中的相应序列在远离铁结合位点的N叶内呈现出带电螺旋和疏水尾部。乳铁杀菌肽与皮肤防御素和蛙皮素之间的序列相似性表明,乳铁杀菌肽可能作为一种两亲性α螺旋发挥作用。