4.6 Article

Tuning the amino acid sequence of minimalist peptides to present biological signals via charge neutralised self assembly

期刊

SOFT MATTER
卷 9, 期 15, 页码 3915-3919

出版社

ROYAL SOC CHEMISTRY
DOI: 10.1039/c3sm27758e

关键词

-

资金

  1. National Health and Medicine Research Council (NHMRC) [APP1020332]
  2. Australian Research Council (ARC) [DP130103131]
  3. Australian Postgraduate Award
  4. NHMRC
  5. Viertel charitable Foundation, Australia
  6. Australian Research Council
  7. Alfred Deakin Research Fellowship

向作者/读者索取更多资源

Nanofibrous materials yielded by the self-assembly of peptides are rich in potential; particularly for the formation of scaffolds that mimic the landscape of the host environment of the cell. Here, we report a novel methodology to direct the formation of supramolecular structures presenting desirable amino acid sequences by the self-assembly of minimalist peptides which cannot otherwise yield the desired scaffold structures under biologically relevant conditions. Through the rational modification of the pKa, we were able to optimise ordered charge neutralised assembly towards in vivo conditions.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.6
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据