Spectroscopic and DLS investigation of polystyrene nanoparticle exposure on Ganglefenum binding to bovine serum albumin
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OpenAlex topics: Protein Interaction Studies and Fluorescence Analysis · Gold and Silver Nanoparticles Synthesis and Applications · Electrostatics and Colloid Interactions
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References (51)
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1. Rajendran D, Chandrasekaran N (2023) Journey of micronanoplastics with blood components. RSC Adv 13:31435–31459. https://doi.org/10.1039/D3RA05620A10.1039/D3RA05620A ↗
2. Luo T, Zhang Y, Wang C, Wang X, Zhou J, Shen M et al (2019) Maternal exposure to different sizes of polystyrene microplastics during gestation causes metabolic disorders in their offspring. Env Poll 295:113122. https://doi.org/10.1016/j.envpol.2019.11312210.1016/j.envpol.2019.113122 ↗
3. Shan S, Zhang Y, Zhaoo H, Zeng T, Zhao X (2022) Polystyrene nanoplastics penetrate across the blood-brain barrier and induce activation of microglia in the brain of mice. Chemosphere 298:134261. https://doi.org/10.1016/j.chemosphere.2022.13426110.1016/j.chemosphere.2022.134261 ↗
4. Cong Y, Baimanov D, Zhou Y, Chen C, Wang L (2022) Penetration and translocation of functional inorganic nanomaterials into biological barriers. Adv Drug Deliv Rev 191:114615. https://doi.org/10.1016/j.addr.2022.11461510.1016/j.addr.2022.114615 ↗
5. Monikh FA, Lehtonen S, Kekalainen J, Karkossa J, Auriola S, Schubert K et al (2024) Biotransformation of nanoplastics in human plasma and their permeation through a model in vivo blood-brain barrier: an in-depth quantive analysis. Nano Today 59:102466. https://doi.org/10.1016/j.nanotod.2024.10246610.1016/j.nanotod.2024.102466 ↗
6. Yang CS, Chang CH, Tsai PJ, Chen WY, Tseng FG, Lo LW (2004) Nanoparticle-based in vivo investigation on blood-brain barrier permeability following ischemia and reperfusion. Anal Chem 76:4465–4471. https://doi.org/10.1021/ac035491v10.1021/ac035491v ↗
7. Mustfa SA, Maurizi E, McGrath J, Chiappini C (2021) Nanomedicine approaches to negotiate local biobarriers for topical drug delivery. Adv Therap 4:2000160. https://doi.org/10.1002/adtp.20200016010.1002/adtp.202000160 ↗
8. Ballesteros S, Domenech J, Barguilla I, Cortés C, Marcos R, Hernández A (2020) Genotoxic and Immunomodulatory Effects in Human White Blood Cells After ex vivo Exposure to Polystyrene Nanoplastics. Envir Sci Nano 7:3431–3446. https://doi.org/10.1039/D0EN00748J10.1039/D0EN00748J ↗
9. Ali N, Katsouli J, Marczylo EL, Gant TW, Wright S, Bernardino de la Serna J (2024) The potential impacts of micro-and-nano plastics on various organ systems in humans. eBioMed 99:104901. https://doi.org/10.1016/j.ebiom.2023.10490110.1016/j.ebiom.2023.104901 ↗
10. Sarma DK, Dubey R, Samarth RM, Shubham S, Chowdhury P, Kumawat M et al (2022) The biological effects of polystyrene nanoplastics on human peripheral blood lymphocyte. Nanomat 12:1632. https://doi.org/10.3390/nano1210163210.3390/nano12101632 ↗
11. Cairns S, Meza-Rojas D, Holliman PJ, Robertson I (2024) Interactions between biochar and nano (micro) plastics in the remediation of aqueous media. Int J Environ Res 18:1–22. https://doi.org/10.1007/s41742-024-00635010.1007/s41742-024-006350 ↗
12. (2002) Report on packaging materials: 2. Polystyrene for food packaging applications. International Life Sciences Institute, p 21
13. Nguyen VN, Lee BJ (2017) Protein corona: a new approach for medicine design. Int J Nanomedicine 12:3137–3151. https://doi.org/10.2147/IJN.SI2930010.2147/IJN.SI29300 ↗
14. Peng Q, Zhang S, Yang Q et al (2013) Performed albumin corona, a protective coating for nanoparticles based drug delivery system. Biomaterials 34:8521–8530. https://doi.org/10.1016/j.biomatrials.2012.07.10210.1016/j.biomatrials.2012.07.102 ↗
15. Kopac T (2021) Protein corona, understanding the nano-particle-protein interaction and future perspectives: a critical review. Int J Biol Macromol 169:1–22. https://doi.org/10.1016/j.ijbiomac.2020.12.10810.1016/j.ijbiomac.2020.12.108 ↗
16. Soliman MG, Martinez-Serra A, Dobricic M, Trinh D, Cheeserman J, Spencer DIR et al (2024) Protocols for isolation and characterization of nanoparticle biomolecular corona complexes. Front Toxicol 3:1–25. https://doi.org/10.3389/ftox.2024.139333010.3389/ftox.2024.1393330 ↗
17. Shirinyan E, Topuzyan V (2011) Gangleron. An effective preparation of wide action spectrum. Pharm1:28. (Article in Russian)
18. Hovhanesyan A (2009) Materials on gangleron preparation. Yerevan (originally published in Russian)
19. Mirzoian SA, Tatevosian SA (1975) Effect of gangleron on the free amino acid content in the gastric mucosa and in the biological fluids of rats with experimental ulcers. Farmakol Toksikol 38:198–200 (Article in Russian)
20. Kubalova MN, Sharpanova IK (1980) Physicochemical basis of the therapeutic use of gangleron electrophoresis by a modulated sinusoidal current in Sympathoganglionitis opr Kurortol Fizioter Lech Fiz Kult 4:20–30 PMID: 6106316 (Article in Russian)
21. Kragh-Hansen U, Chuang VTG, Otagiri M (2002) Practical aspects of the ligand-binding and enzymatic properties of human serum albumin. Biol Pharm Bull 25:695–704. https://doi.org/10.1248/bpb.25.69510.1248/bpb.25.695 ↗
22. Grigoryan K, Shilajyan H, Savvaidis I, Mkhitaryan L, Zatikyan A (2024) Effect of bovine serum albumin on gallic acid and tannic acid radical scavenging properties and binding kinetics with 2,2-diphenyl-1-picrylhydrazyl. Proc Biochem 141:30–38. https://doi.org/10.1016/j.procbio.2024.02.00910.1016/j.procbio.2024.02.009 ↗
23. Larsen TM, Kuhlmann M, Hvam ML, Howard KA (2016) Albumin-based drug delivery: harnessing nature to cure disease. Mol Cell Ther 4:1–12. https://doi.org/10.1186/s40591-016-0048-810.1186/s40591-016-0048-8 ↗
24. Sleep D (2015) Albumin and its application in drug delivery. Expert Opin Drug Deliv 12:793–812. https://doi.org/10.1517/17425247.2015.99331310.1517/17425247.2015.993313 ↗
25. Grigoryan KR, Kazaryan A (2009) Interaction of dimethylsulfoxide and diethylsulfoxide complexes of platinum (II) with bovine serum albumin. J Appl Spect 76:607–610. https://doi.org/10.1007/s10812-009-9241-810.1007/s10812-009-9241-8 ↗
26. Tada D, Tanabe T, Tachibana A, Yamauchi K (2005) Drug release from hydrogel containing albumin as crosslinker. J Biosc Bioeng 100:551–555. https://doi.org/10.1263/jbb.100.55110.1263/jbb.100.551 ↗
27. Wacker M, Chen K, Preuss A, Possemeyer K, Roeder B, Langer C (2010) Photosensitizer loaded HSA nanoparticles. I: preparation and photophysical properties. I J Pharmac 393:253–262. https://doi.org/10.1016/j.ijpharm.2010.04.02210.1016/j.ijpharm.2010.04.022 ↗
28. Du K, Du X, Sun Z, Wang Y, Bao Y, Lan J, Shi R, Zhao Z (2024) Effects of polystyrene nanoplastics on the binding of ciprofloxacin to bovine serum albumin. Colloids Surf A Physicochem Eng Asp 685:133218. https://doi.org/10.1016/j.colsurfa.2024.13321810.1016/j.colsurfa.2024.133218 ↗
29. Leslie H, van Velzen M, Brandsma SH et al (2022) Discovery and quantification of plastic particle pollution in human blood. Environ Int 163:107199. https://doi.org/10.1016/j.envint.2022.10719910.1016/j.envint.2022.107199 ↗
30. Peters T (1996) All about albumin biochemistry. In: Genetics and medical applications. Academic Press, San Diego, CA. https://doi.org/10.1002/food.1997041063110.1002/food.19970410631 ↗
31. Yang F, Zhang Y, Liang H (2014) Interactive association of drugs binding to human serum albumin. I J Mol Sci 15:3580–3595. https://doi.org/10.3390/ijms1503358010.3390/ijms15033580 ↗
32. Pace CN, Vajdos F, Fee L, Grimsley G, Gray T (1995) How to measure and predict the molar absorption coefficient of a protein. Prot Sci 4:2411–2423. https://doi.org/10.1002/pro.556004112010.1002/pro.5560041120 ↗
33. Lorenz-Fonfria VA (2020) Infrared difference spectroscopy of proteins: from bands to bonds. Chem Rev 120:3466–3576. https://doi.org/10.1021/acs.chemrev.9b0044910.1021/acs.chemrev.9b00449 ↗
34. Kong J, Yu S (2007) Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochim Biophys Sin 39:549–559. https://doi.org/10.1111/j.1745-7270.2007.00320.x10.1111/j.1745-7270.2007.00320.x ↗
35. Wani TA, Bakheit AH, Zargar S, Al-Majed AA (2022) Influence of rutin, sinapic acid, and naringenin on binding of tyrosine kinase inhibitor erlotinib to bovine serum albumin using analytical techniques along with computational approach. Appl Sci 12:3575. https://doi.org/10.3390/app1207357510.3390/app12073575 ↗
36. Grigoryan KR, Ghazaryan AG (2013) quenching mechanism of human serum albumin fluorescence by gangleron. Proceed YSU 2:6–10. https://doi.org/10.46991/PYSUB.2013.47.2.00610.46991/PYSUB.2013.47.2.006 ↗
37. Ross PD, Subramanian S (1981) Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20:113096–113102. https://doi.org/10.1021/bi00514a01710.1021/bi00514a017 ↗
38. Hui X, Quanwen L, Ying Z, Yan B, Shuli G (2009) Spectroscopic studies on the interaction of vitamin C with bovine serum albumin. J Sol Chem 38:15–25. https://doi.org/10.1007/s10953-008-9351-610.1007/s10953-008-9351-6 ↗
39. Zhou X, He Z, Huang H (2017) Secondary structure transitions of bovine serum albumin induced by temperature variation. Vibr Spectrosc 92:273–279. https://doi.org/10.1016/j.vibspec.2017.08.00110.1016/j.vibspec.2017.08.001 ↗
40. Grigoryan K, Zatikyan A, Shilajyan H (2021) Effect of monovalent ions on the thermal stability of bovine serum albumin in dimethylsulfoxide aqueous solutions. Spectroscopic approach. J Biomol Struct Dyn 39:2284–2288. https://doi.org/10.1080/07391102.2020.174375910.1080/07391102.2020.1743759 ↗
41. Kong J, Yu S (2007) Fourier transform infrared spectroscopic analysis of protein secondary structures. Acta Biochim Biophys Sin (Shanghai) 39:549–559. https://doi.org/10.1111/j.1745-7270.2007.00320.x10.1111/j.1745-7270.2007.00320.x ↗
42. Lu R, Li WW, Katzir A, Raichlin Y, Yu HQ, Mizaikoff B (2015) Probing the secondary structure of bovine serum albumin during heat-induced denaturation using mid-infrared fiberoptic sensors. Analyst 140:76570. https://doi.org/10.1039/C4AN01495B10.1039/C4AN01495B ↗
43. Nsiah F, McDermott MT (2015) Investigation of adsorption characteristics of fibrinogen on modified gold substrates using infrared reflection absorption spectroscopy, ASRJETS; 14:66–86. https://asrjetsjournal.org/index.php/American_Scientific_Journal/article/view/1078
44. Baier G, Costa C, Zeller A, Baumann D, Sayer C, Araujo PHH, Mailander V, Musyanovych A, Landfester K (2011) BSA adsorption on differently charged polystyrene nanoparticles using isothermal titration calorimetry and the influence on cellular uptake. Macromol Biosci 11:628–638. https://doi.org/10.1002/mabi.20100039510.1002/mabi.201000395 ↗
45. Wangkam T, Yodmongkol S, Disrattakit J, Sutapun B, Amarit R, Somboonkaew A, Srikhirin T (2012) Adsorption of bovine serum albumin (BSA) on polystyrene (PS) and its acid copolymer. Curr Appl Phys 12: 44e52 45. https://doi.org/10.1016/j.cap.2011.04.03910.1016/j.cap.2011.04.039 ↗
46. Cedervall T, Lynch I, Lindman S, Berggard T et al (2007) Understanding the nanoparticle- protein corona using methods to quantify exchange rates and affinities of proteins for nanoparticles. Proc Natl Acad Sci U S A 104:2050–2055. https://doi.org/10.1073/pnas.060858210410.1073/pnas.0608582104 ↗
47. Aggarwal P, Hall JB, McLeland CB, Dobrovolskaia MA, McNeil SE (2009) Nanoparticle interaction with plasma proteins as it relates to particle biodistribution, biocompatibility and therapeutic efficacy. Adv Drug Deliv Rev 61:428–437. https://doi.org/10.1016/j.addr.2009.03.00910.1016/j.addr.2009.03.009 ↗
48. Li Y, Yang G, Mei Z (2012) Spectroscopic and dynamic light scattering studies of the interaction between pterodontic acid and bovine serum albumin. Acta Pharm Sin B 2:53–59. https://doi.org/10.1016/j.apsb.2011.12.00110.1016/j.apsb.2011.12.001 ↗
49. Hadjidemetriou M, Al-Ahmady Z, Kostarelos K (2016) Time-evolution of in vivo protein corona onto blood circulating PEGylated liposomal doxorubicin (DOXIL) nanoparticles. Nanos 8:6948–6957. https://doi.org/10.1039/C5NR09158F10.1039/C5NR09158F ↗
50. Stetefeld J, McKenna SA, Patel TR (2016) Dynamic light scattering a practical guide and applications in biomedical sciences. Biophys Rev 8:409–427. https://doi.org/10.1007/s12551-016-0218-610.1007/s12551-016-0218-6 ↗
51. Tan X, Welsher K (2021) Particle-by-particle in situ characterization of the protein corona via real-time 3D single-particle tracking spectroscopy. Angew Chem I Ed Engl 60:22359–22367. https://doi.org/10.1002/anie.20210574110.1002/anie.202105741 ↗