ANTIMICROBIAL PEPTIDES FROM AMARANTHUS-CAUDATUS SEEDS WITH SEQUENCE HOMOLOGY TO THE CYSTEINE GLYCINE-RICH DOMAIN OF CHITIN-BINDING PROTEINS
ANTIMICROBIAL PEPTIDES FROM AMARANTHUS-CAUDATUS SEEDS WITH SEQUENCE HOMOLOGY TO THE CYSTEINE GLYCINE-RICH DOMAIN OF CHITIN-BINDING PROTEINS
复制标题
DOI：
10.1021/bi00132a023
复制
发表时间：
1992-05-05
期刊：
影响因子：
2.9
通讯作者：
CAMMUE, BPA
中科院分区：
文献类型：
--
作者：
BROEKAERT, WF;MARIEN, W;CAMMUE, BPA
从苋菜（Amaranthuscaudatus）种子中分离得到两种抗菌肽（Ac-AMP 1和Ac-AMP 2），并对其理化性质和生物学特性进行了研究。快原子轰击质谱的基础上，Ac-AMP 1和Ac-AMP 2的单同位素分子量分别为3025和318 1。两种蛋白质的pI值均高于10。Ac-AMP 1的氨基酸序列（29个残基）与Ac-AMP 2的氨基酸序列（30个残基）相同，除了后者在羧基末端有1个额外的残基。这些序列与许多几丁质结合蛋白中富含半胱氨酸/甘氨酸的结构域高度同源。Ac-AMP 1和Ac-AMP 2都以可逆的方式与几丁质结合。Ac-AMP 1和Ac-AMP 2抑制不同植物病原真菌的生长的剂量比其他已知的抗真菌几丁质结合蛋白低得多。此外，它们对革兰氏阳性菌显示出一定的活性。Ac-AMP 1和Ac-AMP 2的抗菌作用被阳离子强烈拮抗。
Two antimicrobial peptides (Ac-AMP1 and Ac-AMP2) were isolated from seeds of amaranth (Amaranthus caudatus), and their physicochemical and biological properties were characterized. On the basis of fast atom bombardment mass spectroscopy, Ac-AMP1 and Ac-AMP2 have monoisotopic molecular masses of 3025 and 318 1, respectively. Both proteins have pI values above 10. The amino acid sequence of Ac-AMP1 (29 residues) is identical to that of Ac-AMP2 (30 residues), except that the latter has 1 additional residue at the carboxyl terminus. The sequences are highly homologous to the cysteine/glycine-rich domain occurring in many chitin-binding proteins. Both Ac-AMP1 and Ac-AMP2 bind to chitin in a reversible way. Ac-AMP1 and Ac-AMP2 inhibit the growth of different plant pathogenic fungi at much lower doses than other known antifungal chitin-binding proteins. In addition, they show some activity on Gram-positive bacteria. The antimicrobial effect of Ac-AMP1 and Ac-AMP2 is strongly antagonized by cations.