In tissue engineering, the relationship between a biomaterial surface and the host's immune response during wound healing is crucial for tissue regeneration. Despite hemoderivative functionalization of biomaterials becoming a common tissue-engineering strategy for enhanced regeneration, the characteristics of the protein-biomaterial interface have not been fully elucidated. This study characterized the interface formed by the adsorbed proteins from various hemoderivatives with pristine and calcium phosphate (CaP)-coated polycaprolactone (PCL) melt electrowritten scaffolds. PCL scaffolds were fabricated by using melt electrospinning writing (MEW). Three hemoderivatives (pure platelet-rich plasma (P-PRP), leucocyte platelet-rich plasma (L-PRP) and injectable platelet-rich fibrin (i-PRF)) and total blood PLASMA (control) were prepared from ovine blood. Hemoderivatives were characterized via SEM/EDX, cross-linking assay, weight loss, pH and protein quantification. The interface between PCL/CaP and hemoderivative was examined via FTIR, XPS and electrophoresis. i-PRF/PCL-CaP (1653 cm), PLASMA/PCL-CaP (1652 cm) and i-PRF/PCL (1651 cm) demonstrated a strong signal at the Amide I region. PLASMA and i-PRF presented similar N1s spectra, with most of the nitrogen involved in N-C=O bonds (≈400 eV). i-PRF resulted in higher adsorption of low molecular weight (LMW) proteins at 60 min, while PLASMA exhibited the lowest adsorption. L-PRP and P-PRP had a similar pattern of protein adsorption. The characteristics of biomaterial interfaces can be customized, thus creating a specific hemoderivative-defined layer on the PCL surface. i-PRF demonstrated a predominant adsorption of LMW proteins. Further investigation of hemoderivative functionalized biomaterials is required to identify the differential protein corona composition, and the resultant immune response and regenerative capacity.
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http://dx.doi.org/10.3390/ijms24076162 | DOI Listing |
J Colloid Interface Sci
December 2024
Key Laboratory for Molecular Enzymology and Engineering, Ministry of Education, School of Life Sciences, Jilin University, Changchun, Jilin 130012, China. Electronic address:
The spontaneous adsorption of proteins onto nanoparticles, known as the protein corona, provides a unique perspective for designing protein-sensing biosensors. This study proposes a tailored protein corona method mediated by Tween-20 and develops a reverse-capture approach for protein quantification assays. The protein-coated microplate captures titanium dioxide nanosheets (TiO-NS) in a phosphate buffer containing Tween-20 and generates fluorescence signals via the photocatalytic reduction of resazurin to resorufin, thereby indicating the amount of protein.
View Article and Find Full Text PDFAnal Chem
December 2024
Analytical & Testing Center, Sichuan University, Chengdu, Sichuan 610064, China.
Spherical nucleic acids (SNAs) usually suffer from an undesired protein corona and disrupt the function of nucleic acids (e.g., aptamer), thereby compromising recognition and response to proteins in the biological environment.
View Article and Find Full Text PDFMol Pharm
December 2024
Department of Chemical Engineering, Dankook University, Yongin-si 16890, South Korea.
The adsorption of plasma proteins (human serum albumin, immunoglobulin γ-1, apolipoproteins A-I and E-III) onto polystyrene surfaces grafted with polyethylene glycol (PEG) at different grafting densities is simulated using an all-atom PEG model validated by comparing the conformations of isolated PEG chains with previous simulation and theoretical values. At high PEG density, the grafted PEG chains extend like brushes, while at low density, they significantly adsorb to the surface due to electrostatic attraction between polystyrene amines and PEG oxygens, forming a PEG layer much thinner than its Flory radius. Free energy calculations show that PEGylation can either increase or decrease the binding strength between proteins and surfaces, to an extent dependent on PEG density and specific proteins involved, in agreement with experiments.
View Article and Find Full Text PDFPhys Chem Chem Phys
December 2024
College of Chemistry and Molecular Sciences, Wuhan University, Wuhan 430072, PR China.
Proteins are some of the most important components in living organisms. When nanoparticles enter a living system, they swiftly interact with proteins to produce the so-called "protein corona", which depicts the adsorption of proteins on large nanoparticles (normally tens to hundreds of nanometers). However, the sizes of small nanoparticles (typically, fluorescent nanomaterials such as quantum dots, noble metal nanoclusters, carbon dots, ) are less than 10 nm, which are comparable or even much smaller than those of proteins.
View Article and Find Full Text PDFInt J Nanomedicine
December 2024
Division of Medical Physics and Biophysics, Gottfried Schatz Research Center for Cell Signaling, Metabolism and Aging, Medical University of Graz, Graz, 8010, Austria.
Background: Selenium (Se) is a vital micronutrient for maintaining homeostasis in the human body. Selenium nanoparticles (SeNPs) have demonstrated improved bioavailability compared to both inorganic and organic forms of Se. Therefore, supplementing with elemental Se in its nano-form is highly promising for biomedical applications related to Se deficiency.
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