β片协同组装控制着两亲肽-聚二乙烯共轭物的分子间取向

IF 1.8 3区 化学 Q4 CHEMISTRY, PHYSICAL
Tarunya Rao Sudarshan , Sujeung Lim , Jeffrey Li , Alicia S. Robang , Leel Mazal Liberty , Herdeline Ann M. Ardoña , Anant K. Paravastu
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引用次数: 0

摘要

在这项研究中,我们阐明了刺激响应肽-聚二乙烯(PDA)共轭物的结构组织,这种共轭物可在中性水溶液条件下自组装成一维纳米结构。氨基酸序列在肽段的外围带有正电荷或负电荷域,以提高在水中的溶解度,同时还能推动单个和组合成分组装成 β 片。PDA 的光聚合以及由此产生的聚合物材料的光学特性对外部刺激的敏感性,在很大程度上取决于两亲肽-二乙炔单元组装成一维纳米结构的结构组织。对 13C 标记和 15N 标记样品进行的固态核磁共振测量表明,带正电荷和带负电荷的两亲肽都能进行自组装,但自组装更倾向于反平行的 β 片状结构。当带正电荷和带负电荷的两亲肽在等比溶液中相互作用时,合作共组装比自组装占优势,从而产生了理想的平行β片结构,同时增加了结构的有序性。这些结果表明,合理放置带相反电荷的残基可以控制肽双亲化合物共组装中的β链组织,这将对刺激响应型生物材料(如本文研究的肽-PDAs)的适应性产生影响。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Cooperative β-sheet coassembly controls intermolecular orientation of amphiphilic peptide-polydiacetylene conjugates

Cooperative β-sheet coassembly controls intermolecular orientation of amphiphilic peptide-polydiacetylene conjugates

In this work, we elucidated the structural organization of stimuli-responsive peptide-polydiacetylene (PDA) conjugates that can self-assemble as 1D nanostructures under neutral aqueous conditions. The amino acid sequences bear positively or negatively charged domains at the periphery of the peptide segments to promote solubility in water while also driving assembly of the individual and combined components into β-sheets. The photopolymerization of PDA, as well as the sensitivity of the resulting optical properties of the polymeric material to external stimuli, highly depends on the structural organization of the assembly of amphiphilic peptide-diacetylene units into 1D-nanostructures. Solid-state NMR measurements on 13C-labeled and 15N-labeled samples show that positively charged and negatively charged peptide amphiphiles are each capable of self-assembly, but self-assembly favors antiparallel β-sheet structure. When positively and negatively charged peptide amphiphiles interact in stoichiometric solutions, cooperative coassembly dominates over self-assembly, resulting in the desired parallel β-sheet structure with a concomitant increase in structural order. These results reveal that rational placement of oppositely charged residues can control β-strand organization in a peptide amphiphile coassembly, which would have implications on the adaptive properties of stimuli-responsive biomaterials such as the peptide-PDAs studied here.

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来源期刊
CiteScore
5.30
自引率
9.40%
发文量
42
审稿时长
72 days
期刊介绍: The journal Solid State Nuclear Magnetic Resonance publishes original manuscripts of high scientific quality dealing with all experimental and theoretical aspects of solid state NMR. This includes advances in instrumentation, development of new experimental techniques and methodology, new theoretical insights, new data processing and simulation methods, and original applications of established or novel methods to scientific problems.
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