Secondary Structure Formation and LCST Behavior of Short Elastin-Like Peptides
Secondary Structure Formation and LCST Behavior of Short Elastin-Like Peptides
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DOI：
10.1021/bm800784y
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发表时间：
2008-10-01
影响因子：
6.2
通讯作者：
Klok, Harm-Anton
中科院分区：
文献类型：
--
作者：
Nuhn, Harald;Klok, Harm-Anton
这篇文章研究了基于GVGVP基序的短弹性蛋白样肽库的二级结构和LCST行为的链长和化学组成的影响。圆二色谱实验表明，大多数研究的肽显示出典型的弹性蛋白构象行为，随着温度的升高，无规卷曲减少，β-转角特征增加。对于几种肽，在含有10 mg/mL肽的NaCl水溶液中观察到LCST行为。通过外推的LCST在不同的NaCl浓度下测得的零盐浓度，表观LCST确定。发现表观LCST随着肽链长度的增加而降低，这与预测分配系数的趋势相关性很好。肽的表观LCST可以通过用更疏水的异亮氨酸、亮氨酸或苯丙氨酸残基连续替换缬氨酸残基来操纵。在一个特定的系列的变体中，发现表观LCST随着缬氨酸置换数量的增加而降低，这也与分配系数的预测演变相关。虽然相对重要性的整体肽的疏水性和构象上的LCST行为的组成氨基酸的偏好仍然是一个悬而未决的问题，在这方面的贡献中描述的结果清楚地表明，短，弹性蛋白样肽是潜在的有吸引力的积木的一系列材料的应用在生物医学和工程。
This contribution investigates the effects of chain length and chemical composition on the secondary structure and LCST behavior of a library of short, elastin-like peptides based on the GVGVP motif. CD experiments revealed that most of the investigated peptides showed the typical elastin conformational behavior with a decrease in random coil and an increase in beta-turn character with increasing temperature. For several peptides, LCST behavior was observed in aqueous NaCl solutions containing 10 mg/mL peptide. By extrapolation of the LCSTs measured at different NaCl concentrations to zero-salt concentration, apparent LCSTs were determined. The apparent LCST was found to decrease with increasing peptide chain length, which correlated well with the trend in the predicted partition coefficients. The apparent LCST of the peptides could be manipulated by successive replacement of the valine residues by more hydrophobic isoleucine, leucine, or phenylalanine residues. Within a particular series of variants, the apparent LCST was found to decrease with an increasing number of valine replacements, which also correlated well with the predicted evolution of the partition coefficient. Although the relative importance of the overall peptide hydrophobicity and the conformational preferences of the constituent amino acids on the LCST behavior still remains an open question, the results described in this contribution clearly demonstrate that short, elastin-like peptides are potentially attractive building blocks for a range of materials applications in biomedicine and engineering.