Selsted M E, Harwig S S, Ganz T, Schilling J W, Lehrer R I
J Clin Invest. 1985 Oct;76(4):1436-9. doi: 10.1172/JCI112121.
The primary structures of three human neutrophil antimicrobial peptides (HNP) were determined. The peptides, HNP-1, HNP-2, and HNP-3, which we have termed defensins, were rich in cystine, arginine, and aromatic residues, but were devoid of free sulfhydryl groups and carbohydrate moieties. They were 29-30 residues in length and identical in sequence in all but their amino terminal residues. The defensins were homologous in sequence to peptides of similar size and biological activity previously purified from rabbit polymorphonuclear leukocytes, but unrelated to other neutrophil proteins of known sequence. 11 amino acid residues of the human defensins, including all six cysteinyl residues, were invariantly conserved in the six rabbit members of this multigene peptide family. That similarly structured antimicrobial peptides are present in both rabbit and human leukocytes supports their purported role as cidal agents in phagocyte-mediated host defense.
三种人中性粒细胞抗菌肽（HNP）的一级结构已被确定。我们称为防御素的这些肽，即HNP-1、HNP-2和HNP-3，富含胱氨酸、精氨酸和芳香族残基，但不含游离巯基和碳水化合物部分。它们长度为29 - 30个残基，除了氨基末端残基外，序列完全相同。这些防御素在序列上与先前从兔多形核白细胞中纯化出的大小和生物活性相似的肽同源，但与已知序列的其他中性粒细胞蛋白无关。人类防御素的11个氨基酸残基，包括所有6个半胱氨酰残基，在这个多基因肽家族的6个兔成员中是不变地保守的。兔和人白细胞中都存在结构相似的抗菌肽，这支持了它们在吞噬细胞介导的宿主防御中作为杀伤剂的假定作用。
