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.
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References
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)
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)
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)
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)
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)
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)
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)
Ahmadian, E., Eftekhari, A., Janas, D., Vahedi, P.: Nanofiber scaffolds based on extracellular matrix for articular cartilage engineering: a perspective. Nanotheranostics. 7, 61 (2023)
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)
Hornok, V.: Serum albumin nanoparticles: problems and prospects. Polymers 13, 3759 (2021)
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)
Nasibova, A.: Generation of nanoparticles in biological systems and their application prospects. Adv Biol Earth Sci. 8, 140–146 (2023)
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)
Khalilov R.: A comprehensive review of advanced nano-biomaterials in regenerative medicine and drug delivery. Adv. Biol. Earth Sci. 8, 5–18 (2023)
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)
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)
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)
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)
Dubeau, S., Bourassa, P., Thomas, T.J., Tajmir-Riahi, H.A.: Biogenic and synthetic polyamines bind bovine serum albumin. Biomacromol 11, 1507–1515 (2010)
Mandeville, J.S., Tajmir-Riahi, H.A.: Complexes of dendrimers with bovine serum albumin. Biomacromol 11, 465–472 (2010)
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)
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)
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)
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)
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)
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)
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)
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)
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)
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)
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The authors thank the Shandong Provincial Natural Science Foundation (ZR2022MH320) for the financial support.
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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.
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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
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DOI: https://doi.org/10.1007/s10847-023-01217-x