Sequence-dependent gelation kinetics of β-hairpin peptide hydrogels.
Sequence-dependent gelation kinetics of β-hairpin peptide hydrogels.
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DOI：
10.1021/ma901423n
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发表时间：
2009-11-10
期刊：
影响因子：
5.5
通讯作者：
Furst EM
中科院分区：
文献类型：
--
作者：
Larsen TH;Branco MC;Rajagopal K;Schneider JP;Furst EM
采用多粒子跟踪微流变学和圆二色性（CD）光谱表征了四种β-发夹寡肽的凝胶动力学，这些β-发夹寡肽被设计为对环境条件（如pH、离子强度和温度）的变化表现出响应行为。这些肽主要是缬氨酸和赖氨酸残基的交替序列，不同之处在于靠近II型β-转角序列的单个氨基酸的点取代。对于减少肽总电荷的点取代，凝胶化速率变得更快。类似地，增加离子强度减少或屏蔽分子内和分子间的静电排斥，再次导致更快的凝胶化动力学。CD测量表明，在凝胶点处折叠肽的浓度随着凝胶化动力学变慢而降低，这可能表明组装速率与所得凝胶微观结构之间的关系。最后，一个模型是基于静电势垒肽折叠和协会同意半定量与微观流变学的结果。这代表了理解肽电荷和物理化学条件在这些肽水凝胶因子的自组装中的作用的第一步。
The gelation kinetics of four β-hairpin oligopeptides that have been designed to exhibit responsive behavior to changes in environmental conditions, such as pH, ionic strength and temperature, are characterized using multiple particle tracking microrheology and circular dichroism (CD) spectroscopy. The peptides, predominantly an alternating sequence of valine and lysine residues, differ by a point substitution of a single amino acid near a type II’β-turn sequence. The rate of gelation becomes faster for point substitutions which reduce the total charge of the peptide. Similarly, increasing the ionic strength reduces or screens intra- and inter-molecular electrostatic repulsions, again leading to faster gelation kinetics. CD measurements show that the concentration of folded peptide at the gel point decreases as the gelation kinetics become slower, possibly indicating a relationship between the assembly rate and the resulting gel microstructure. Finally, a model is developed based on the electrostatic barrier to peptide folding and association which agrees semi-quantitatively with the microrheology results. This represents a first step towards understanding the role of peptide charge and physico-chemical conditions in the self-assembly of these peptide hydrogelators.
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影响因子：
14
作者：
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影响因子：
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DOI：
10.1073/pnas.0701980104
发表时间：
2007-05-08
影响因子：
11.1
作者：
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DOI：
10.1073/pnas.0600559103
发表时间：
2006-03-28
影响因子：
11.1
作者：
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通讯作者：
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