Sulfanilic acid inspired self-assembled fibrous materials

详细信息    查看全文

• 作者：Christopher Narh ; Guohui Li ; Qingqing Wang ; Fenglin Huang…
• 刊名：Colloid & Polymer Science
• 出版年：2016
• 出版时间：September 2016
• 年：2016
• 卷：294
• 期：9
• 页码：1483-1494
• 全文大小：1,643 KB
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Polymer Sciences
  Physical Chemistry
  Soft Matter and Complex Fluids
  Characterization and Evaluation Materials
  Food Science
  
• 出版者：Springer Berlin / Heidelberg
• ISSN：1435-1536
• 卷排序：294

文摘

The exploration of the potentials of peptide in drug delivery has led to numerous studies in peptide synthesis involving different protocols depending on the expected final products. In this study, we explored the self-assembling behavior of sulfanilic acid by reacting it with two hydrophobic amino acids namely valine and alanine using the linear polypeptide synthesis protocol. The reaction consequently resulted in bonding together of linear fibrous structures. Results on scanning electron microscope revealed that the individual fibers separated upon the introduction of aniline, an increased length and further observation showing that the fibers were altered into four different structures. Results on X-ray diffraction revealed that amide C-N bond in a peptide was found to be shorter than the C-N bond in a simple amine and residue backbone dihedral angles of around −60° and −45° in α-helix formation, while the dramatic rotation around the N2_C2_ bond resulted in tube. On the other hand, results on atomic force microscopy (AFM) revealed a fairly rough surface, while differential scanning calorimeter (DSC) results indicated that, at Tg (85 °C), the fibers underwent endothermic decomposition of about −2.5 mg and experienced an exothermic recrystallization at 125 °C. Results on thermogravimetric analysis (TGA) confirmed that the fiber was stable at 180 °C.KeywordsSulfanilic acidHydrophobic amino acidsSelf-assemblyPolypeptide synthesis