Skip to main content
Log in

The synthesis of hydroxyethyl starch 130/0.4-loaded albumin nanoparticles: biocompatibility and interaction mechanism

  • Original Article
  • Published:
Journal of Inclusion Phenomena and Macrocyclic Chemistry Aims and scope Submit manuscript

Abstract

The nanoplatform for drugs demonstrates favorable stability and high therapeutical advantages in the bloodstream. Here, by using hydroxyethyl starch (HES) 130/0.4 and serum albumin, which were widely used as volume expanders in intravenous therapy, we synthesized a new HES 130/0.4-loaded bovine serum albumin (BSA) nanoparticles and investigated the binding mechanism in the simulated physiological environment with considerations of compatibility. Analysis of the fluorescence quenching data of BSA by HES using the Stern–Volmer equation proved the formation of a 1:1 ground state complex. The binding parameters (ΔS° = 329 J mol−1 K−1, ΔH° = 6.38 × 105 J mol−1, and ΔG = − 3.04 × 105 J mol−1) at body temperature manifested that the interaction was exothermic and driven by hydrophobic interactions. The binding distance was calculated as 2.73 nm and showed a high possibility of Förster resonance energy transfer. The structural alterations of BSA were assessed both qualitatively and quantitatively through the application of 3D/synchronous fluorescence and circular dichroism techniques, respectively, which showed adaptive changes in secondary structures. The results presented in this study offer not only novel ideas of albumin-based NP synthesis, but precise and comprehensive primary data that elucidate the mechanisms of HES-BSA interaction, helping to comprehend its pharmacodynamics in blood.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6
Fig. 7
Fig. 8

Similar content being viewed by others

References

  1. Martin, C., Jacob, M., Vicaut, E., Guidet, B., Van Aken, H., Kurz, A.: Effect of waxy maize-derived hydroxyethyl starch 130/0.4 on renal function in surgical patients. Anesthesiology 118, 387–394 (2013)

    Article  CAS  PubMed  Google Scholar 

  2. Lagny, M.-G., Roediger, L., Koch, J.-N., Dubois, F., Senard, M., Donneau, A.-F., Hubert, M.B., Hans, G.A.: Hydroxyethyl starch 130/0.4 and the risk of acute kidney injury after cardiopulmonary bypass: a single-center retrospective study. J. Cardiothorac. Vasc. Anesth. 30, 869–875 (2016)

    Article  CAS  PubMed  Google Scholar 

  3. Vives, M., Callejas, R., Duque, P., Echarri, G., Wijeysundera, D., Hernandez, A., Sabate, A., Bes-Rastrollo, M., Monedero, P., GEDRCC: Modern hydroxyethyl starch and acute kidney injury after cardiac surgery: a prospective multicentre cohort. Br. J. Anaesth. 117, 458–463 (2016)

    Article  CAS  PubMed  Google Scholar 

  4. Wong, Y.L., Lautenschläger, I., Zitta, K., Schildhauer, C., Parczany, K., Röcken, C., Steinfath, M., Weiler, N., Albrecht, M.: Adverse effects of hydroxyethyl starch (HES 130/0.4) on intestinal barrier integrity and metabolic function are abrogated by supplementation with albumin. J. Transl. Med. 14, 1–11 (2016)

    Article  CAS  Google Scholar 

  5. Wei, L., Li, D., Sun, L.: The comparison of albumin and 6% hydroxyethyl starches (130/0.4) in cardiac surgery: a meta-analysis of randomized controlled clinical trials. BMC Surg. 21, 1–10 (2021)

    Article  Google Scholar 

  6. Zhao, X., Lu, D., Hao, F., Liu, R.: Exploring the diameter and surface dependent conformational changes in carbon nanotube-protein corona and the related cytotoxicity. J. Hazard. Mater. 292, 98–107 (2015)

    Article  CAS  PubMed  Google Scholar 

  7. Zhao, Z., Li, H., Yao, J., Lan, J., Bao, Y., Zhao, L., Zong, W., Zhang, Q., Hollert, H., Zhao, X.: Binding of tetrabromobisphenol A and S to human serum albumin is weakened by coexisting nanoplastics and environmental kosmotropes. Environ. Sci. Technol. 57, 4464–4470 (2023)

    Article  CAS  PubMed  Google Scholar 

  8. Ahmadian, E., Eftekhari, A., Janas, D., Vahedi, P.: Nanofiber scaffolds based on extracellular matrix for articular cartilage engineering: a perspective. Nanotheranostics. 7, 61 (2023)

    Article  PubMed  PubMed Central  Google Scholar 

  9. Tao, H.-y, Wang, R.-q, Sheng, W.-j, Zhen, Y.-s: The development of human serum albumin-based drugs and relevant fusion proteins for cancer therapy. Int. J. Biol. Macromol. 187, 24–34 (2021)

    Article  CAS  PubMed  Google Scholar 

  10. Hornok, V.: Serum albumin nanoparticles: problems and prospects. Polymers 13, 3759 (2021)

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  11. Shen, X., Liu, X., Li, T., Chen, Y., Chen, Y., Wang, P., Zheng, L., Yang, H., Wu, C., Deng, S.: Recent advancements in serum albumin-based nanovehicles toward potential cancer diagnosis and therapy. Front. Chem. 9, 746646 (2021)

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  12. Nasibova, A.: Generation of nanoparticles in biological systems and their application prospects. Adv Biol Earth Sci. 8, 140–146 (2023)

    Google Scholar 

  13. Baran, A., Fırat Baran, M., Keskin, C., Hatipoğlu, A., Yavuz, Ö., İrtegün Kandemir, S., Adican, M.T., Khalilov, R., Mammadova, A., Ahmadian, E.: Investigation of antimicrobial and cytotoxic properties and specification of silver nanoparticles (AgNPs) derived from Cicer arietinum L. green leaf extract. Front. Bioeng. Biotechnol. 10, 855136 (2022)

    Article  PubMed  PubMed Central  Google Scholar 

  14. Khalilov R.: A comprehensive review of advanced nano-biomaterials in regenerative medicine and drug delivery. Adv. Biol. Earth Sci. 8, 5–18 (2023)

  15. Zhao, X., Lu, D., Liu, Q.S., Li, Y., Feng, R., Hao, F., Qu, G., Zhou, Q., Jiang, G.: Hematological effects of gold nanorods on erythrocytes: hemolysis and hemoglobin conformational and functional changes. Adv. Sci. 4, 1700296 (2017)

    Article  Google Scholar 

  16. Zhao, X.C., Liu, R.T., Chi, Z.X., Teng, Y., Qin, P.F.: New insights into the behavior of bovine serum albumin adsorbed onto carbon nanotubes: comprehensive spectroscopic studies. J. Phys. Chem. B 114, 5625–5631 (2010)

    Article  CAS  PubMed  Google Scholar 

  17. Song, S., Li, Y., Liu, Q.S., Wang, H., Li, P., Shi, J., Hu, L., Zhang, H., Liu, Y., Li, K.: Interaction of mercury ion (Hg2+) with blood and cytotoxicity attenuation by serum albumin binding. J. Hazard. Mater. 412, 125158 (2021)

    Article  CAS  PubMed  Google Scholar 

  18. Pan, J., Ye, Z., Cai, X., Wang, L., Cao, Z.: Biophysical study on the interaction of ceftriaxone sodium with bovine serum albumin using spectroscopic methods. J. Biochem. Mol. Toxicol. 26, 487–492 (2012)

    Article  CAS  PubMed  Google Scholar 

  19. Dubeau, S., Bourassa, P., Thomas, T.J., Tajmir-Riahi, H.A.: Biogenic and synthetic polyamines bind bovine serum albumin. Biomacromol 11, 1507–1515 (2010)

    Article  CAS  Google Scholar 

  20. Mandeville, J.S., Tajmir-Riahi, H.A.: Complexes of dendrimers with bovine serum albumin. Biomacromol 11, 465–472 (2010)

    Article  CAS  Google Scholar 

  21. Sharma, D., Ojha, H., Pathak, M., Singh, B., Sharma, N., Singh, A., Kakkar, R., Sharma, R.K.: Spectroscopic and molecular modelling studies of binding mechanism of metformin with bovine serum albumin. J. Mol. Struct. 1118, 267–274 (2016)

    Article  CAS  Google Scholar 

  22. Zhao, Z., Li, G., Liu, Q.S., Liu, W., Qu, G., Hu, L., Long, Y., Cai, Z., Zhao, X., Jiang, G.: Identification and interaction mechanism of protein corona on silver nanoparticles with different sizes and the cellular responses. J. Hazard. Mater. 414, 125582 (2021)

    Article  CAS  PubMed  Google Scholar 

  23. Zhao, X., Hao, F., Lu, D., Liu, W., Zhou, Q., Jiang, G.: Influence of the surface functional group density on the carbon-nanotube-induced α-chymotrypsin structure and activity alterations. ACS Appl. Mater. Interfaces 7, 18880–18890 (2015)

    Article  CAS  PubMed  Google Scholar 

  24. Zhao, X., Li, P., Song, S., Wang, H., Zhao, L., Zong, W., Zhang, H., Qu, G., Hu, L., Cai, Z.: Molecular structural heterogeneity of bisphenols governs their serum albumin binding. Sci. Total. Environ. 781, 146499 (2021)

    Article  CAS  Google Scholar 

  25. Mokaberi, P., Babayan-Mashhadi, F., Amiri Tehrani Zadeh, Z., Saberi, M.R., Chamani, J.: Analysis of the interaction behavior between nano-curcumin and two human serum proteins: combining spectroscopy and molecular stimulation to understand protein-protein interaction. J. Biomol. Struct. Dyn. 39, 3358–3377 (2021)

    CAS  PubMed  Google Scholar 

  26. Zhao, Z., Yao, J., Li, H., Lan, J., Hollert, H., Zhao, X.: Interaction of polystyrene nanoplastics and hemoglobin is determined by both particle curvature and available surface area. Sci. Total. Environ. 899, 165617 (2023)

    Article  CAS  PubMed  Google Scholar 

  27. Zhang, Y.Z., Li, H.R., Dai, J., Chen, W.J., Zhang, J., Liu, Y.: Spectroscopic studies on the binding of Cobalt(II) 1,10-phenanthroline complex to bovine serum albumin. Biol. Trace Elem. Res. 135, 136–152 (2010)

    Article  CAS  PubMed  Google Scholar 

  28. Ashoka, S., Seetharamappa, J., Kandagal, P., Shaikh, S.: Investigation of the interaction between trazodone hydrochloride and bovine serum albumin. J. Lumin. 121, 179–186 (2006)

    Article  CAS  Google Scholar 

  29. Lu, D.W., Zhao, X.C., Zhao, Y.C., Zhang, B.C., Zhang, B., Geng, M.Y., Liu, R.T.: Binding of Sudan II and Sudan IV to bovine serum albumin: comparison studies. Food Chem. Toxicol. 49, 3158–3164 (2011)

    Article  CAS  PubMed  Google Scholar 

  30. Zhao, X., Liu, R., Teng, Y., Liu, X.: The interaction between Ag(+) and bovine serum albumin: a spectroscopic investigation. Sci. Total. Environ. 409, 892–897 (2011)

    Article  CAS  PubMed  Google Scholar 

Download references

Funding

The authors thank the Shandong Provincial Natural Science Foundation (ZR2022MH320) for the financial support.

Author information

Authors and Affiliations

Authors

Contributions

H.W. and S.H. wrote the main manuscript text and J.Z. prepared all the figures. J.L. and M.L. provided the experimental sources. All authors reviewed the manuscript.

Corresponding author

Correspondence to Jie Li.

Ethics declarations

Conflict of interest

The authors declare no conflict of interest.

Ethical approval

This paper does not contain any studies with human participants or animals performed by any authors.

Additional information

Publisher's Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Wang, H., Huang, S., Zhang, J. et al. The synthesis of hydroxyethyl starch 130/0.4-loaded albumin nanoparticles: biocompatibility and interaction mechanism. J Incl Phenom Macrocycl Chem 104, 73–81 (2024). https://doi.org/10.1007/s10847-023-01217-x

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10847-023-01217-x

Keywords

Navigation