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Effect of sonication on a novel designed peptide

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Abstract

The reassembly of a half-sequence ionic self-complementarity peptide CH3CO-Pro-Ser-Phe-Cys-Phe-Lys-Phe-Glu-Pro-NH2 was reported, which could self-assemble into stable nanofibers and formed hydrogel consisting of >99% water. In this study, the nanofiber scaffold was sonicated by an ultrasonic cell disruptor. The effects of sonication were detected by circular dichroism (CD), atomic force microscopy (AFM), and rheology. AFM image illustrated that the sonicated fragments could quickly reassemble into nanofibers, while the morphology was distinguishable from the original one. CD spectrum revealed that the conversion occurred mainly between regular β-strand structure and distorted β-strand structure. Rheological analyses showed that the storage modulus (G′) of the peptide solution at the 7th day after sonication decreased by nearly 40% compared with the value of the solution before sonication. Finally, a plausible conversion model was proposed to interpret the reassembly process.

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Authors and Affiliations

  1. School of Chemical Engineering, Sichuan University, Chengdu, 610065, China

    Liping Ruan  (阮丽萍)

  2. West China Hospital Laboratory of Nanomedicine and West China Hospital Institute for Nanobiomedical Technology and Membrane Biology, Sichuan University, Chengdu, 610041, China

    Hanlin Luo & Hangyu Zhang

  3. Laboratory of Ethnopharmacology, Institute for Nanobiomedical Technology and Membrane Biology, Regenerative Medicine Research Center, West China Hospital, West China Medical School, Sichuan University, Chengdu, 610041, China

    Zhihua Xing

Authors
  1. Liping Ruan  (阮丽萍)
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  2. Hanlin Luo
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  3. Hangyu Zhang
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  4. Zhihua Xing
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Corresponding author

Correspondence to Liping Ruan  (阮丽萍).

Additional information

Funded by the National Natural Science Foundation of China (No. 51003065) and New Teachers’ Fund for Doctor Stations, Ministry of Education (No. 20100181120077)

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Ruan, L., Luo, H., Zhang, H. et al. Effect of sonication on a novel designed peptide. J. Wuhan Univ. Technol.-Mat. Sci. Edit. 28, 622–626 (2013). https://doi.org/10.1007/s11595-013-0741-2

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  • DOI: https://doi.org/10.1007/s11595-013-0741-2

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