Solvent-dependent structure of two tryptophan-rich antimicrobial peptides and their analogs studied by FTIR and CD spectroscopy
Solvent-dependent structure of two tryptophan-rich antimicrobial peptides and their analogs studied by FTIR and CD spectroscopy
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DOI：
10.1016/j.bbamem.2006.07.013
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发表时间：
2006-10-01
影响因子：
3.4
通讯作者：
Prenner, Elmar J.
中科院分区：
文献类型：
--
作者：
Andrushchenko, Valery V.;Vogel, Hans J.;Prenner, Elmar J.
采用傅立叶变换红外光谱（FTIR）和圆二色谱（CD）相结合的方法研究了一系列抗菌肽在不同溶剂中的结构变化。沿着几种tritrpticin类似物，包括Tritrp 1（tritrpticin的酰胺化类似物）、Tritrp 2（Tritrp 1的类似物，具有Arg -> Lys取代）、Tritrp 3（Tritrp 1的类似物，具有Pro -> Ala取代）和Tritrp 4（Trittp 1的类似物，具有Trp -> Tyr取代），研究了充分表征的和有效的抗微生物肽indolicidin和tritrpticin。所有的肽进行了研究，在水性缓冲液中，乙醇和十二烷基磷酸胆碱（DPC）胶束的存在下。结果表明，tritypticin及其类似物优先采用转弯结构在所有溶剂中的研究。与indolicidin相比，由结合到DPC胶束的tritrpticin类似物形成的转角结构更紧凑并且构象更受限。虽然几种肽在乙醇中显示出轻微的α-螺旋构象倾向，但这种趋势仅对Tritrp 3很强，其也采用了具有DPC胶束的大部分α-螺旋结构。Tritrp 3也表现出沿着Tritrp 1与DPC胶束相互作用的最高能力，而Tritrp 2和Tritrp 4表现出最弱的相互作用。(c)2006 Elsevier B. V.保留所有权利。
Structural changes for a series of antimicrobial peptides in various solvents were investigated by a combined approach of FTIR and CD spectroscopy. The well-characterized and potent antimicrobial peptides indolicidin and tritrpticin were studied along with several analogs of tritrpticin, including Tritrp1 (amidated analog of tritrpticin), Tritrp2 (analog of Tritrp1 with Arg -> Lys substitutions), Tritrp3 (analog of Tritrp1 with Pro -> Ala substitutions) and Tritrp4 (analog of Trittp1 with Trp -> Tyr substitutions). All peptides were studied in aqueous buffer, ethanol and in the presence of dodecylphosphocholine (DPC) micelles. It was shown that tritypticin and its analogs preferentially adopt turn structures in all solvents studied. The turn structures formed by the tritrpticin analogs bound to DPC micelles are more compact and more conformationally restricted compared to indolicidin. While several peptides showed a slight propensity for an (x-helical conformation in ethanol, this trend was only strong for Tritrp3, which also adopted a largely alpha-helical structure with DPC micelles. Tritrp3 also demonstrated along with Tritrp1 the highest ability to interact with DPC micelles, while Tritrp2 and Tritrp4 showed the weakest interaction. (c) 2006 Elsevier B.V. All rights reserved.