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Effect of temperature on self-assembly of an ionic tetrapeptide

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Abstract

The self-aggregation of the ionic tetrapeptide RWDW (R = arginine, W = tryptophan, D = aspartic acid) was studied at three temperatures (15, 25 and 35 °C) by different experimental techniques such as atomic force microscopy (AFM), isothermal titration calorimetry (ITC) and differential scanning calorimetry (DSC). AFM was used to investigate the morphology of the aggregates; the AFM images at 15 °C showed the presence of a dense network of entangled fibres, while at 35 °C the peptide assembled into sparse globular and fibrillar structures. Moreover, the calorimetric experiments showed that in all cases the disaggregation process is endothermic and dependent on the investigated temperature. Both the enthalpy of disaggregation and the cac change with temperature. In particular, at 35 °C, we obtained the lower enthalpy of disaggregation and higher cac, showing that the disaggregation process is favoured at high temperature. The DSC scans strengthen the hypothesis that the RWDW aggregation is a rather complex phenomenon.

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References

  1. Zhang S. Emerging biological materials through molecular selfassembly. Biotechnol Adv. 2002;20:321–39.

    Article  CAS  Google Scholar 

  2. Reches M, Gazit E. Rigid, self-assembled hydrogel composed of a modified aromatic dipeptide. Curr Nanosci. 2006;2:105–11.

    Article  CAS  Google Scholar 

  3. Lomakin A, Teplow DB, Kirschner DA, Benedek GB. Kinetic theory of fibrillogenesis of amyloid β–protein. Proc Natl Acad Sci USA. 1997;94:7942–7.

    Article  CAS  Google Scholar 

  4. Dobson CM. Protein folding and its links with human disease. Biochem Soc Symp. 2001;68:1–26.

    CAS  Google Scholar 

  5. Yu L, Ding J. Injectable hydrogels as unique biomedical materials. Chem Soc Rev. 2008;37:1473–81.

    Article  CAS  Google Scholar 

  6. Holmes TC, de Lacalle S, Su X, Liu G, Rich A, Zhang S. Extensive neurite outgrowth and active synapse formation on self-assembling peptide scaffolds. Proc Natl Acad Sci USA. 2000;97:6728–33.

    Article  CAS  Google Scholar 

  7. Deming TJ. Synthetic polypeptides for biomedical applications. Prog Polym Sci. 2007;32:858–75.

    Article  CAS  Google Scholar 

  8. Hosseinkhani H, Hosseinkhani M, Kobayashi H. Design of tissue-engineered nanoscaffold through self-assembly of peptide amphiphile. J Bioact Compat Polym. 2006;21:277–96.

    Article  CAS  Google Scholar 

  9. Zhang S, Holmes TC, Lockshin C, Rich A. Spontaneous assembly of a self-complementary oligopeptide to form a stable macroscopic membrane. Proc Natl Acad Sci USA. 1993;90:3334–8.

    Article  CAS  Google Scholar 

  10. Desii A, Chiellini F, Duce C, Ghezzi L, Monti S, Solaro R, Tiné MR. Influence of structural features on the self-assembly of short ionic oligopeptide. J Polym Sci Part A: Polym Chem. 2010;48:889–97.

    Article  CAS  Google Scholar 

  11. Desii A, Duce C, Ghezzi L, Monti S, Solaro R, Tiné MR. Investigation of the self-assembly of hydrophobic self-complementary ionic tetrapeptides. J Therm Anal Cal. 2009;97:789–90.

    Article  Google Scholar 

  12. Desii A, Chiellini F, Di Stefano R, Tiné MR, Solaro R. Hydrogel scaffolds by self-Assembly of a complementary ionic tetrapeptide. J Polym Sci Part A: Polym Chem. 2010;48:986–90.

    Article  CAS  Google Scholar 

  13. Pochan DJ, Schneider JP, Kretsinger J, Ozbas B, Rajagopal K, Haines L. Thermally reversible hydrogels via intramolecular folding and consequent self-assembly of a de novo designed peptide. J Am Chem Soc. 2003;125(39):11802–3.

    Article  CAS  Google Scholar 

  14. Jeong B, Bae YH, Lee DS, Kim SW. Biodegradable block copolymers as injectable drug-delivery systems. Nature. 1997;388:860–2.

    Article  CAS  Google Scholar 

  15. Privalov PL. Stability of protein-structure and hydrophobic interactions. Biol Chem Hoppe Seyler. 1988;369:199.

    Google Scholar 

  16. Ye Z, Zhang H, Luo H, Wang S, Zhou Q, DU X, Tang C, Chen L, Liu J, Shi YK, Zhang EY, Ellis-Behnke R, Zhao X. Temperature and pH effects on biophysical and morphological properties of self-assembling peptide RADA16-I. J Pept Sci. 2008;14:152–62.

    Article  CAS  Google Scholar 

  17. Ramachandran S, Taraban MB, Trewhella J, Gryczynski I, Gryczynski Z, Yu YB. Effect of temperature during assembly on the structure and mechanical properties of peptide-based materials. Biomacromolecules. 2010;11:1502–6.

    Article  CAS  Google Scholar 

  18. Garidel P, Hildebrand A. Thermodynamic properties of association colloids. J Therm Anal Cal. 2005;82:483–9.

    Article  CAS  Google Scholar 

  19. Majhi RP, Blume A. Thermodynamic characterization of temperature-induced micellization and demicellization of detergents studied by differential scanning calorimetry. Langmuir. 2001;17:3844–51.

    Article  CAS  Google Scholar 

  20. Kljin JE, Kevelam J, Engberts JBFN. Aggregation behavior of mono-endcapped hydrophobically modified poly(sodium acrylate)s in aqueous solution. J Coll Interf Sci. 2000;226:76–82.

    Article  Google Scholar 

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Acknowledgements

The authors are grateful to the reviewer for helpful suggestions. The financial support by MIUR, INSTM and Fondazione Cassa di Risparmio di Pisa is gratefully acknowledged.

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Correspondence to M. R. Tiné.

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Tiné, M.R., Alderighi, M., Duce, C. et al. Effect of temperature on self-assembly of an ionic tetrapeptide. J Therm Anal Calorim 103, 75–80 (2011). https://doi.org/10.1007/s10973-010-1060-x

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