Correction to "Tuning chemistry and topography of nanoengineered surfaces to manipulate immune response for bone regeneration applications"

After online publication of this Article, the authors noticed an error in the Supplementary Figure 3 lower magnification of 38AApp SEM image. The correct Supplementary Figure 3 of this Article should have appeared as below. The authors apologize for any inconvenience caused. (Figure Presented).</p

Protein Interactions with Nanoengineered Polyoxazoline Surfaces Generated via Plasma Deposition

Protein adsorption to biomaterials is critical in determining their suitability for specific applications, such as implants or biosensors. Here, we show that surface nanoroughness can be tailored to control the covalent binding of proteins to plasma-deposited polyoxazoline (PPOx). Nanoengineered surfaces were created by immobilizing gold nanoparticles varying in size and surface density on PPOx films. To keep the surface chemistry consistent while preserving the nanotopography, all substrates were overcoated with a nanothin PPOx film. Bovine serum albumin was chosen to study protein interactions with the nanoengineered surfaces. The results demonstrate that the amount of protein bound to the surface is not directly correlated with the increase in surface area. Instead, it is determined by nanotopography-induced geometric effects and surface wettability. A densely packed array of 16 and 38 nm nanoparticles hinders protein adsorption compared to smooth PPOx substrates, while it increases for 68 nm nanoparticles. These adaptable surfaces could be used for designing biomaterials where proteins adsorption is or is not desirable

The introduction of nanotopography suppresses bacterial adhesion and enhances osteoinductive capacity of plasma deposited polyoxazoline surface

The plasma deposited polyoxazoline (PPOx) has been emerging in biomedical applications, especially for the surface modification of bone tissue engineering scaffold and/or bone implants. Herein, PPOx surfaces were generated by plasma polymerization with the introduction of surface nanotopography gradient, achieved by immobilization of different density of 16 nm gold nanoparticles. The introduction of surface nanotopography suppressed the adhesion of S. aureus on PPOx surface. Moreover, the introduction of surface nanotopography enhanced the initial attachment and spreading of hMSCs, as well as promoted the osteogenic differentiation of hMSCs. RhoA/ROCK signaling pathway may be involved in the enhancement of osteoinductive capacity of PPOx surface by nanotopography

Ultra-small gold nanoclusters assembled on plasma polymer-modified zeolites : A multifunctional nanohybrid with anti-haemorrhagic and anti-inflammatory properties

Hemostatic agents are pivotal for managing clinical and traumatic bleeding during emergency and domestic circumstances. Herein, a novel functional hybrid nanocomposite material consisting of plasma polymer-modified zeolite 13X and ultra-small gold nanoclusters (AuNCs) was fabricated as an efficient hemostatic agent. The surface of zeolite 13X was functionalised with amine groups which served as binding sites for carboxylate terminated AuNCs. Protein corona studies revealed the enhanced adsorption of two proteins, namely, coagulation factors and plasminogen as a result of AuNCs immobilization on the zeolite surface. The immune response studies showed that the hybrid nanocomposites are effective in reducing inflammation, which combined with a greater attachment of vitronectin, may promote wound healing. The hemostatic potential of the nanocomposite could be directly correlated with their immunomodulatory and anti-haemorrhagic properties. Together, the hybrid nanoengineered material developed in this work could provide a new avenue to tackle life-threatening injuries in civilian and other emergencies.</p

Plasma polymerized bio-interface directs fibronectin adsorption and functionalization to enhance “epithelial barrier structure” formation via FN-ITG β1-FAK-mTOR signaling cascade

Background: Transepithelial medical devices are increasing utilized in clinical practices. However, the damage of continuous natural epithelial barrier has become a major risk factor for the failure of epithelium-penetrating implants. How to increase the “epithelial barrier structures” (focal adhesions, hemidesmosomes, etc.) becomes one key research aim in overcoming this difficulty. Directly targeting the in situ “epithelial barrier structures” related proteins (such as fibronectin) absorption and functionalization can be a promising way to enhance interface-epithelial integration. Methods: Herein, we fabricated three plasma polymerized bio-interfaces possessing controllable surface chemistry. Their capacity to adsorb and functionalize fibronectin (FN) from serum protein was compared by Liquid Chromatography-Tandem Mass Spectrometry. The underlying mechanisms were revealed by molecular dynamics simulation. The response of gingival epithelial cells regarding the formation of epithelial barrier structures was tested. Results: Plasma polymerized surfaces successfully directed distinguished protein adsorption profiles from serum protein pool, in which plasma polymerized allylamine (ppAA) surface favored adsorbing adhesion related proteins and could promote FN absorption and functionalization via electrostatic interactions and hydrogen bonds, thus subsequently activating the ITG β1-FAK-mTOR signaling and promoting gingival epithelial cells adhesion. Conclusion: This study offers an effective perspective to overcome the current dilemma of the inferior interface-epithelial integration by in situ protein absorption and functionalization, which may advance the development of functional transepithelial biointerfaces. Graphical Abstract: Tuning the surface chemistry by plasma polymerization can control the adsorption of fibronectin and functionalize it by exposing functional protein domains. The functionalized fibronectin can bind to human gingival epithelial cell membrane integrins to activate epithelial barrier structure related signaling pathway, which eventually enhances the formation of epithelial barrier structure.</p