Journal
SOFT MATTER
Volume 10, Issue 31, Pages 5656-5661Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c4sm01065e
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Funding
- Danish National Research Foundation
- Danish Research Agency through iNANO Center
- Danish Research Council
- VKR Young Investigator Program in Denmark
- Sino-Danish Center for Education and Research
- Villum Fonden [00007194] Funding Source: researchfish
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The final structure and properties of synthetic peptides mainly depend on their sequence composition and experimental conditions. This work demonstrates that a variation in the positions of hydrophobic residues within a peptide sequence can tune the self-assembly. Techniques employed are atomic force microscopy, transmission electron microscopy and an innovative method based on surface acoustic waves. In addition, a systematic investigation on pH dependence was carried out by utilizing constant experimental parameters.
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