| Autor: |
Baruah K; Department of Chemistry, National Institute of Technology Meghalaya, Shillong 793003, India., Singh AK; Department of Molecular Biology and Biotechnology, Tezpur University, Napaam, Tezpur 784028, Assam, India., Kumari K; Department of Bioscience and Bioengineering, Indian Institute of Technology Guwahati, Guwahati 781039, Assam India., Nongbri DL; Department of Biotechnology & Bioinformatics, North-Eastern Hill University, Shillong 793022, India., Jha AN; Department of Molecular Biology and Biotechnology, Tezpur University, Napaam, Tezpur 784028, Assam, India., Singha Roy A; Department of Chemistry, National Institute of Technology Meghalaya, Shillong 793003, India. |
| Jazyk: |
angličtina |
| Zdroj: |
Langmuir : the ACS journal of surfaces and colloids [Langmuir] 2024 Jan 16; Vol. 40 (2), pp. 1381-1398. Date of Electronic Publication: 2023 Dec 30. |
| DOI: |
10.1021/acs.langmuir.3c03032 |
| Abstrakt: |
In order to better understand the bioavailability and biocompatibility of polyphenol-assisted surface-modified bioengineered nanoparticles in nanomedicine applications, here, we address a series of photophysical experiments to quantify the binding affinity of serum albumin toward polyphenol-capped gold nanoparticles. For this, two different gold nanoparticles (AuNPs) were synthesized via the green synthesis approach, where curcumin and turmeric extract act as reducing as well as capping agents. The size, surface charge, and surface plasmon bands of the AuNPs were highly affected by the adsorption of human serum albumin (HSA) during protein corona formation, which was investigated using dynamic light scattering (DLS), ξ-potential, ultraviolet-visible (UV-vis) spectroscopy, and transmission electron microscopy (TEM) measurements. Fluorescence-based methods, absorbance, and SERS experiments were carried out to evaluate the binding aspects of AuNPs with HSA. We found that the AuNPs show moderate binding affinity toward HSA ( K b ∼ 10 4 M -1 ), irrespective of the capping agents on the surface. Hydrophobic association, along with some contribution of electrostatic interaction, played a key role in the binding process. The binding interaction was more toward the subdomain IIA region of HSA, as indicated by the competitive displacement studies using site-specific binders (warfarin and flufenamic acid). Because of the large surface curvature of small-sized AuNPs, the secondary structural conformations of HSA were slightly altered, as revealed by circular dichroism (CD), Fourier transform infrared (FT-IR) spectroscopy, and surface-enhanced Raman scattering (SERS) measurements. Additionally, the findings of the binding interactions were re-evaluated using molecular dynamics (MD) simulation studies by determining the root-mean-square deviation (RMSD), root-mean-square fluctuation (RMSF), radius of gyration ( R g ), and changes in the binding energy of HSA upon complexation with AuNPs. To determine the tentative evidence for pharmacokinetic administration, these biocompatible AuNPs were applied to inhibit the amyloid fibril formation of HSA and monitored by using the thioflavin T (ThT) assay, ANS fluorescence assay, fluorescence microscopic imaging, and FESEM. AuNPs were found to show better resistance toward fibrillation of the adsorbed protein. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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