Modification of gelation kinetics in bioactive peptide amphiphiles.
Modification of gelation kinetics in bioactive peptide amphiphiles.
复制标题
生物活性肽两亲物中凝胶化动力学的修饰。
DOI：
10.1016/j.biomaterials.2008.07.049
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发表时间：
2008-12
期刊：
影响因子：
14
通讯作者：
Stupp, Samuel I.
中科院分区：
文献类型：
--
作者：
Niece, Krista L.;Czeisler, Catherine;Sahni, Vibhu;Tysseling-Mattiace, Vicki;Pashuck, Eugene T.;Kessler, John A.;Stupp, Samuel I.
以前在我们的实验室中设计的肽两亲物（PAS）是自我组装成在体外和体内都表现出生物活性的纳米纤维。自组装可以通过电荷中和或盐介导的肽序列中带电残基的筛选触发，而所得纳米纤维可以以低至0.5％的重量浓度形成宏观凝胶。在保留纳米纤维的生物活性的同时，控制凝胶化的动力学对于为特定的临床应用定制这些材料至关重要。我们在这里报告了一系列的PA，其肽序列的变化导致了不同的凝胶化速率，而无需更改生物活性段。在更疏水性PA的溶液状态下，氢键的聚集体的先前存在似乎加速了凝胶化动力学。肽序列的突变包括更多的亲水性和笨重的氨基酸抑制这些核的形成，并通过纳米纤维网络的自组装有效地减慢了凝胶化。在不破坏生物活性的情况下修饰自组装系统中凝胶化动力学的能力对于再生医学的可注射疗法很重要。
Peptide amphiphiles (PAs) previously designed in our laboratory are known to self-assemble into nanofibers that exhibit bioactivity both in vitro and in vivo. Self-assembly can be triggered by charge neutralization or salt-mediated screening of charged residues in their peptide sequences, and the resulting nanofibers can form macroscopic gels at concentrations as low as 0.5% by weight. Controlling the kinetics of gelation while retaining the bioactivity of nanofibers could be critical in tailoring these materials for specific clinical applications. We report here on a series of PAs with different rates of gelation resulting from changes in their peptide sequence without changing the bioactive segment. The pre-existence of hydrogen-bonded aggregates in the solution state of more hydrophobic PAs appears to accelerate gelation kinetics. Mutation of the peptide sequence to include more hydrophilic and bulky amino acids suppresses formation of these nuclei and effectively slows down gelation through self-assembly of the nanofiber network. The ability to modify gelation kinetics in self-assembling systems without disrupting bioactivity could be important for injectable therapies in regenerative medicine.
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