An origami-based technique for simple, effective and inexpensive fabrication of highly aligned far-field electrospun fibers.

Fabrication of highly aligned fibers by far-field electrospinning is a challenging task to accomplish. Multiple studies present advances in the alignment of electrospun fibers which involve modification of the conventional electrospinning setup with complex additions, multi-phased fabrication, and expensive components. This study presents a new collector design with an origami structure to produce highly-aligned far-field electrospun fibers. The origami collector mounts on the rotating drum and can be easily attached and removed for each round of fiber fabrication. This simple, effective, and inexpensive technique yields high-quality ultra-aligned fibers while the setup remains intact for other fabrication types. The electrospun poly(ɛ-caprolactone) (PCL) fibers were assessed by scanning electron microscope (SEM), fiber diameter distribution, water contact angle (WCA), Fast Fourier Transform analysis (FFT), surface plot profile, and pixel intensity plots. We thoroughly explored the impact of influential parameters, including polymer concentration, injection rate, collector rotation speed, distance from the collector to the tip, and needle gauge number on fibers' quality and alignment. Moreover, we employed machine learning algorithms to predict the outcomes and classify the high-quality fibers instead of low-quality productions.

Polymethacrylate Coated Electrospun PHB Fibers as a Functionalized Platform for Bio-Diagnostics: Confirmation Analysis on the Presence of Immobilized IgG Antibodies against Dengue Virus.

In this article, a combination of far field electrospinning (FFES) and free-radical polymerization has been used to create a unique platform for protein immobilization via the physical attachment of biomolecules to the surface of the fiber mats. The large specific surface area of the fibers with its tailored chemistry provides a desirable platform for effective analyte-surface interaction. The detailed analysis of protein immobilization on a newly developed bio-receptive surface plays a vital role to gauge its advantages in bio-diagnostic applications. We relied on scanning electron microscopy (SEM), diameter range analysis, and X-ray photoelectron spectroscopy (XPS), along with thermal gravimetric analysis (TGA), water-in-air contact angle analysis (WCA), Fourier transform infrared spectroscopy (FTIR), and atomic force microscopy (AFM) to study our developed platforms and to provide valuable information regarding the presence of biomolecular entities on the surface. Detailed analyses of the fiber mats before and after antibody immobilization have shown obvious changes on the surface of the bioreceptive surface including: (i) an additional peak corresponding to the presence of an antibody in TGA analysis; (ii) extra FTIR peaks corresponding to the presence of antibodies on the coated fiber platforms; and (iii) a clear alteration in surface roughness recorded by AFM analysis. Confirmation analyses on protein immobilization are of great importance as they underlay substantial grounds for various biosensing applications.