Polymorphism in peptide self-assembly visualized.
Polymorphism in peptide self-assembly visualized.
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多肽自组装的多态性可视化。
DOI：
10.1073/pnas.2123197119
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发表时间：
2022-02-08
影响因子：
11.1
通讯作者：
Tirrell M
中科院分区：
文献类型：
--
作者：
Tirrell M
基于精确定位、精细平衡和弱（相对于 kT）的组装亚基之间的相互作用，自发形成明确的超分子结构，是自组装的一个有用定义。人们认识到蛋白质可以从变性状态自发地重折叠 (1)，这表明组装蛋白质三级结构所需的信息已内置于一级结构中，这是自组装过程的生物学重要性和力量的早期指标。自发热力学意味着沿着自由能梯度向下移动，寻求全局最小值，但是，当然，这并不意味着动态瞬时。自组装过程具有移动和采样复杂自由能景观的路径、动力学和其他复杂性，并且并不总是落在全局自由能最小值处，例如与蛋白质错误折叠相关的病理学就证明了这一点 (2)。通过自组装将天然和非天然蛋白质和肽组织成胶束、片材、小管、纤维、丝和其他多分子结构，受到与单个蛋白质分子折叠类似的影响，也发生在自然界中并通过合成分子工程。肽的超分子组装通常具有工程疏水性、手性或其他修饰，已被证明可用于制造材料 (3)、疫苗 (4) 和治疗药物，Pieri 等人 (5) 在 PNAS 论文中举例说明，其中由合成八肽 Lanreotide 形成的组装结构已通过低温透射电子显微镜 (cryo-TEM) 以高分辨率确定。兰瑞肽类似于一种称为生长抑素的天然化学物质，生长抑素在体内由下丘脑产生，其功能尤其是调节垂体分泌生长激素。这种合成激素类似物产生的纳米管组件，当透皮递送时，可以保护其免受酶促降解，并随着时间的推移缓慢释放治疗肽。一般来说，肽的自组装可以通过多种方式增强其单个肽成分的特性和性能。对肽（例如源自细胞外基质蛋白的肽）进行疏水性修饰，通常会形成延伸的、缠结的、蠕虫状或杆状胶束网络，这些胶束表现出细胞粘附或其他信号传导活性，而这些活性无法单独从肽中获得 (6)。肽自组装可保护抗菌肽免受
The spontaneous formation of well-defined supramolecular structures, based on precisely located, finely balanced, and weak, relative to kT, interactions among the assembling subunits, is a useful definition of self-assembly. The recognition that proteins could spontaneously refold from their denatured states (1), demonstrating that the information required to assemble the tertiary structure of a protein is built into the primary structure, was an early indicator of the biological importance and power of self-assembly processes. Spontaneous thermodynamically means moving down a free energy gradient seeking a global minimum, but, of course, it does not mean instantaneous dynamically. Selfassembly processes have pathways, kinetics, and other intricacies of moving over and sampling complex free energy landscapes, and do not always land in the global free energy minimum, demonstrated, for example, by the pathologies related to protein misfolding (2). Organization of native and unnatural proteins and peptides into micelles, sheets, tubules, fibers, filaments, and other multimolecular structures by self-assembly, subject to similar influences as folding of individual protein molecules, also happens in nature and via synthetic molecular engineering. The supramolecular assembly of peptides, often with engineered hydrophobicity, chirality, or other modifications, has proven useful in making materials (3), vaccines (4), and therapeutics, exemplified in the PNAS paper by Pieri et al.(5), in which the structure of the assembly formed from the synthetic octapeptide Lanreotide has been determined at high resolution by cryotransmission electron microscopy (cryo-TEM). Lanreotide is similar to a natural chemical called somatostatin, which is produced in the body by the hypothalamus and functions inter alia to modulate the secretion of growth hormone by the pituitary gland. The nanotube assembly created by this synthetic hormone analog, when delivered transdermally, serves to protect it from enzymatic degradation and to release the therapeutic peptide slowly over time. In general, self-assembly of peptides can enhance the properties and performance of their individual peptide constituents in numerous ways. Hydrophobic modification of peptides, such as those derived from extracellular matrix proteins, often leads to networks of extended, entangled, worm-or rod-like micelles displaying cell adhesion or other signaling activities that could not readily be obtained from the peptides alone (6). Peptide self-assembly defends antimicrobial peptides from
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影响因子：
17.1
作者：
Rubinov, Boris;Wagner, Nathaniel;Ashkenasy, Gonen
通讯作者：
Ashkenasy, Gonen
影响因子：
2
作者：
Hayles MF;DE Winter DAM
通讯作者：
DE Winter DAM
DOI：
10.1073/pnas.1615025114
发表时间：
2017-04-04
影响因子：
11.1
作者：
Zhao, Haiyan;Li, Kunpeng;Tang, Liang
通讯作者：
Tang, Liang
影响因子：
6.2
作者：
Sathaye S;Zhang H;Sonmez C;Schneider JP;MacDermaid CM;Von Bargen CD;Saven JG;Pochan DJ
通讯作者：
Pochan DJ
DOI：
10.1073/pnas.1730609100
发表时间：
2003-09-02
影响因子：
11.1
作者：
Valéry, C;Paternostre, M;Artzner, F
通讯作者：
Artzner, F