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仅由D-氨基酸构成的自组装肽d-EAK16的结构动力学

Structural dynamic of a self-assembling peptide d-EAK16 made of only D-amino acids.

作者信息

Luo Zhongli, Zhao Xiaojun, Zhang Shuguang

机构信息

West China Hospital, Laboratory for Nanobiomedical Technology, Sichuan University, Chengdu, Sichuan, China.

出版信息

PLoS One. 2008 May 28;3(5):e2364. doi: 10.1371/journal.pone.0002364.

DOI:10.1371/journal.pone.0002364
PMID:18509542
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2387071/
Abstract

We here report systematic study of structural dynamics of a 16-residue self-assembling peptide d-EAK16 made of only D-amino acids. We compare these results with its chiral counterpart L-form, l-EAK16. Circular dichroism was used to follow the structural dynamics under various temperature and pH conditions. At 25 degrees C the d-EAK16 peptide displayed a typical beta-sheet spectrum. Upon increasing the temperature above 70 degrees C, there was a spectrum shift as the 218 nm valley widens toward 210 nm. Above 80 degrees C, the d-EAK16 peptide transformed into a typical alpha-helix CD spectrum without going through a detectable random-coil intermediate. When increasing the temperature from 4 degrees C to 110 degrees C then cooling back from 110 degrees C to 4 degrees C, there was a hysteresis: the secondary structure from beta-sheet to alpha-helix and then from alpha-helix to beta-sheet occurred. d-EAK16 formed an alpha-helical conformation at pH0.76 and pH12 but formed a beta-sheet at neutral pH. The effects of various pH conditions, ionic strength and denaturing agents were also noted. Since D-form peptides are resistant to natural enzyme degradation, such drastic structural changes may be exploited for fabricating molecular sensors to detect minute environmental changes. This provides insight into the behaviors of self-assembling peptides made of D-amino acids and points the way to designing new peptide materials for biomedical engineering and nanobiotechnology.

摘要

我们在此报告了对一种仅由D-氨基酸构成的16个残基的自组装肽d-EAK16的结构动力学的系统研究。我们将这些结果与其手性对应物L型l-EAK16进行了比较。利用圆二色性来追踪在各种温度和pH条件下的结构动力学。在25℃时，d-EAK16肽呈现出典型的β-折叠光谱。当温度升高到70℃以上时，随着218nm处的谷向210nm变宽，光谱发生了移动。在80℃以上，d-EAK16肽转变为典型的α-螺旋CD光谱，且未经过可检测到的无规卷曲中间体。当温度从4℃升高到110℃，然后从110℃冷却回4℃时，出现了滞后现象：二级结构从β-折叠转变为α-螺旋，然后又从α-螺旋转变为β-折叠。d-EAK16在pH0.76和pH12时形成α-螺旋构象，但在中性pH时形成β-折叠。还注意到了各种pH条件、离子强度和变性剂的影响。由于D型肽对天然酶降解具有抗性，这种剧烈的结构变化可用于制造分子传感器以检测微小的环境变化。这为深入了解由D-氨基酸构成的自组装肽的行为提供了见解，并为生物医学工程和纳米生物技术设计新型肽材料指明了方向。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6263/2387071/3bcf98121eac/pone.0002364.g012.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6263/2387071/cd266295a4a8/pone.0002364.g006.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6263/2387071/82dfe1114fbb/pone.0002364.g009.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6263/2387071/d11ecddfc140/pone.0002364.g011.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6263/2387071/3bcf98121eac/pone.0002364.g012.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6263/2387071/2e4c970f6b77/pone.0002364.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6263/2387071/559f0f9bfbeb/pone.0002364.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6263/2387071/cd266295a4a8/pone.0002364.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6263/2387071/fee045d63c79/pone.0002364.g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6263/2387071/291ab5e6fad8/pone.0002364.g008.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6263/2387071/c8b74a998d0f/pone.0002364.g010.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6263/2387071/3bcf98121eac/pone.0002364.g012.jpg

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