Antimicrobial properties of amyloid peptides.
Antimicrobial properties of amyloid peptides.
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DOI：
10.1021/mp200419b
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发表时间：
2012-04-02
影响因子：
4.9
通讯作者：
Nussinov R
中科院分区：
文献类型：
--
作者：
Kagan BL;Jang H;Capone R;Teran Arce F;Ramachandran S;Lal R;Nussinov R
20多种被称为淀粉样病的临床综合征的特征是组织中广泛的不溶性纤维沉积。这些无定形的刚果红染色沉积物被称为淀粉样蛋白，表现出典型的绿色双折射和交叉β结构。大量证据表明，淀粉样蛋白的寡聚中间体在这些慢性疾病状态的发病机制中是有毒的物种。越来越多的数据表明，这些有毒物质在细胞膜上形成离子通道，导致钙稳态被破坏，膜去极化，能量排出，在某些情况下还会发生细胞凋亡。淀粉样多肽通道具有许多共同的生物学特性，包括普遍的U型β-Strand-Turn-β链结构、不可逆性和自发插入膜、产生大的异质性单通道电导、相对较差的离子选择性、刚果红的抑制和锌的通道阻断。最近的证据表明，数量增加的淀粉样蛋白不仅对宿主靶细胞有毒性，而且还具有抗菌活性。此外，至少有一种人类抗菌肽-1，它通过通道形成机制杀死微生物，已被证明具有形成延长的淀粉样纤维的能力，非常类似于经典的致病淀粉样蛋白。在本文中，我们将回顾已报道的淀粉样蛋白的抗菌特性，以及这些发现对我们理解淀粉样蛋白结构和功能的意义。
More than two dozen clinical syndromes known as amyloid diseases are characterized by the buildup of extended insoluble fibrillar deposits in tissues. These amorphous Congo red staining deposits known as amyloids exhibit a characteristic green birefringence and cross-β structure. Substantial evidence implicates oligomeric intermediates of amyloids as toxic species in the pathogenesis of these chronic disease states. A growing body of data has suggested that these toxic species form ion channels in cellular membranes causing disruption of calcium homeostasis, membrane depolarization, energy drainage, and in some cases apoptosis. Amyloid peptide channels exhibit a number of common biological properties including the universal U-shape β-strand-turn-β-strand structure, irreversible and spontaneous insertion into membranes, production of large heterogeneous single-channel conductances, relatively poor ion selectivity, inhibition by Congo red, and channel blockade by zinc. Recent evidence has suggested that increased amounts of amyloids are not only toxic to its host target cells but also possess antimicrobial activity. Furthermore, at least one human antimicrobial peptide, protegrin-1, which kills microbes by a channel-forming mechanism, has been shown to possess the ability to form extended amyloid fibrils very similar to those of classic disease-forming amyloids. In this paper, we will review the reported antimicrobial properties of amyloids and the implications of these discoveries for our understanding of amyloid structure and function.
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影响因子：
4.3
作者：
ARISPE, N;POLLARD, HB;ROJAS, E
通讯作者：
ROJAS, E
影响因子：
4.1
作者：
Araki-Sasaki, K;Ando, Y;Tanihara, H
通讯作者：
Tanihara, H
DOI：
10.1073/pnas.0335642100
发表时间：
2003-03-04
影响因子：
11.1
作者：
Fernández, A;Berry, RS
通讯作者：
Berry, RS
影响因子：
15.9
作者：
Fraser, SP;Suh, YH;Djamgoz, MBA
通讯作者：
Djamgoz, MBA
影响因子：
5.6
作者：
Bokvist, M;Lindström, F;Gröbner, G
通讯作者：
Gröbner, G