Macromolecular Research

, Volume 17, Issue 8, pp 597–602 | Cite as

Investigation on structure and properties of a novel designed peptide

  • Li-Ping Ruan
  • Han-Lin Luo
  • Hang-Yu Zhang
  • Xiaojun Zhao


Although the existing design principle of full-sequence ionic complement is convenient for the development of peptides, it greatly constrains the exploration of peptides with other possible assembly mechanisms and different yet essential functions. Herein, a novel designed half-sequence ionic complementary peptide (referred to as P9), AC-Pro-Ser-Phe-Asn-Phe-Lys-Phe-Glu-Pro-NH2, is reported. When transferred from pure water to sodium chloride solution, P9 underwent a dramatic morphological transformation from globular aggregations to nanofibers. Moreover, the rheological experiment showed that the P9 could form a hydrogel with a storage modulus of about 30 Pa even at very low peptide concentration (0.5% (wt/vol)). The P9 hydrogel formed in salt solution could recover in a period of about 1,800 sec, which is faster than that in the pure water. The data suggested that the half-sequence, ionic complementary peptide might be worthy of further research for its special properties.


peptide half-sequence ionic complement sodium chloride conformation fiber hydrogel 


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Copyright information

© The Polymer Society of Korea and Springer 2009

Authors and Affiliations

  • Li-Ping Ruan
    • 1
  • Han-Lin Luo
    • 1
  • Hang-Yu Zhang
    • 1
  • Xiaojun Zhao
    • 1
  1. 1.Institute for Nanobiomedical Technology and Membrane Biology, West China HospitalSichuan UniversityChengdu, SichuanPR China

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