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真核生物来源的阴离子型抗菌肽。

Anionic antimicrobial peptides from eukaryotic organisms.

机构信息

School of Forensic and Investigative Science, University of Central Lancashire Preston PR1 2HE, UK.

出版信息

Curr Protein Pept Sci. 2009 Dec;10(6):585-606. doi: 10.2174/138920309789630589.

DOI:10.2174/138920309789630589
PMID:19751192
Abstract

Anionic antimicrobial peptides / proteins (AAMPs) were first reported in the early 1980s and since then, have been established as an important part of the innate immune systems of vertebrates, invertebrates and plants. These peptides are active against bacteria, fungi, viruses and pests such as insects. AAMPs may be induced or expressed constitutively and in some cases, antimicrobial activity appears to be a secondary role for these peptides with other biological activities constituting their primary role. Structural characterization shows AAMPs to generally range in net charge from -1 to -7 and in length from 5 residues to circa 70 residues and for a number of these peptides, post-translational modifications are essential for antimicrobial activity. Membrane interaction appears key to the antimicrobial function of AAMPs and to facilitate these interactions, these peptides generally adopt amphiphilic structures. These architectures vary from the alpha-helical peptides of some amphibians to the cyclic cystine knot structures observed in some plant proteins. Some AAMPs appear to use metal ions to form cationic salt bridges with negatively charged components of microbial membranes, thereby facilitating interaction with their target organisms, but in many cases, the mechanisms underlying the antimicrobial action of these peptides are unclear or have not been elucidated. Here, we present an overview on current research into AAMPs, which suggests that these peptides are an untapped source of putative antimicrobial agents with novel mechanisms of action and possess potential for application in the medical and biotechnological arenas.

摘要

阴离子抗菌肽/蛋白(AAMPs)于 20 世纪 80 年代初首次被报道,从那时起,它们已被确立为脊椎动物、无脊椎动物和植物先天免疫系统的重要组成部分。这些肽类对细菌、真菌、病毒和昆虫等害虫具有活性。AAMPs 可以诱导或组成型表达,在某些情况下,抗菌活性似乎是这些肽类的次要作用,而其他生物活性构成其主要作用。结构特征表明,AAMPs 的净电荷通常在-1 到-7 之间,长度从 5 个残基到约 70 个残基不等,对于其中一些肽类,翻译后修饰对于抗菌活性是必不可少的。膜相互作用似乎是 AAMPs 抗菌功能的关键,为了促进这些相互作用,这些肽类通常采用两亲性结构。这些结构从一些两栖动物的α-螺旋肽到一些植物蛋白中观察到的环状半胱氨酸结结构。一些 AAMPs 似乎利用金属离子与微生物膜的带负电荷的成分形成正电荷盐桥,从而促进与靶生物的相互作用,但在许多情况下,这些肽类的抗菌作用机制尚不清楚或尚未阐明。在这里,我们对当前关于 AAMPs 的研究进行了综述,这表明这些肽类是具有新型作用机制的潜在抗菌剂的未开发来源,并有可能应用于医学和生物技术领域。

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