Despite extensive research, current methods for creating three-dimensional (3D) silk fibroin (SF) scaffolds lack control over molecular rearrangement, particularly in the formation of β-sheet nanocrystals that severely embrittle SF, as well as hierarchical fiber organization at both micro- and macroscale. Here, we introduce a fabrication process based on electrowriting of aqueous SF solutions followed by post-processing using an aqueous solution of sodium dihydrogen phosphate (NaHPO). This approach enables gelation of SF chains controlled β-sheet formation and partial conservation of compliant random coil structures. Moreover, this process allows for precise architecture control in microfiber scaffolds, enabling the creation of 3D flat and tubular macro-geometries with square-based and crosshatch microarchitectures, featuring inter-fiber distances of 400 μm and ∼97% open porosity. Remarkably, the crosslinked printed structures demonstrated a balanced coexistence of β-sheet and random coil conformations, which is uncommon for organic solvent-based crosslinking methods. This synergy of printing and post-processing yielded stable scaffolds with high compliance (modulus = 0.5-15 MPa) and the ability to support elastic cyclic loading up to 20% deformation. Furthermore, the printed constructs supported adherence and growth of human renal epithelial and endothelial cells with viability above 95%. These cells formed homogeneous monolayers that aligned with the fiber direction and deposited type-IV collagen as a specific marker of healthy extracellular matrix, indicating that both cell types attach, proliferate, and organize their own microenvironment within the SF scaffolds. These findings represent a significant development in fabricating organized stable SF scaffolds with unique microfiber structures and mechanical and biological properties that make them highly promising for tissue engineering applications.
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http://dx.doi.org/10.1039/d4bm00624k | DOI Listing |
J Phys Chem Lett
December 2024
Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, 100190, China.
Light-harvesting complex II (LHCII), the most abundant membrane protein in photosystem II, plays dual roles, i.e., efficient light harvesting and energy transfer to the reaction center under low light conditions and dissipating excess energy as heat to prevent photodamage under high irradiation conditions.
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December 2024
Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India.
Nucleocapsid protein (N) of SARS-CoV-2 is a multivalent protein, which is responsible for viral replication, assembly, packaging and modulates host immune response. In this study, we report conformational measurements of N protein at different pH by observing transition in secondary and tertiary structural contents by biophysical and computational approaches. Spectroscopic measurements revealed that N protein loses its secondary and tertiary structure at extreme acidic pH while maintaining its native conformation at mild acidic and alkaline pH.
View Article and Find Full Text PDFJ Med Chem
December 2024
Biochemistry and Structural Biology Division, CSIR-Central Drug Research Institute, Sector 10, Jankipuram Extension, Sitapur Road, Lucknow 226031, India.
The quest for new approaches for generating novel bioactive designer proteins/peptides has continued with their success in various biomedical applications. Previously, we designed a 14-mer α-helical peptide with antimicrobial and antimycobacterial activities by employing a tandem repeat of the 7-mer, "KVLGRLV" human chemerin segment. Herein, we devised a new method of "sliding framework" with this segment to create amino acid scaffolds of varying sizes and sequences and explored the design of a peptide library with antibacterial and antimycobacterial activities.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
College of Food Science, Northeast Agricultural University, Harbin 150030, China. Electronic address:
Induction electric field (IEF) technology is a new green treatment technology based on electric field, and its application has not been widely reported, especially in the direction of soybean protein isolate (SPI) modification. Therefore, IEF and several commonly used physical modification methods were used to investigate the effect on the structure and interfacial properties of SPI. The IEF treatment was found to be superior to the other groups in terms of emulsification performance, solubility and flexibility, which were enhanced by 44.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
School of Materials Science and Engineering, Zhengzhou University, Zhengzhou 450001, PR China; Archeology Innovation Center, Zhengzhou University, Zhengzhou 450001, PR China. Electronic address:
In this study, CA-Gel complexes were prepared by crosslinking gelatin with chlorogenic acid (CA) by EDC/NHS chemistry, and incorporated into gelatin to produce CA-Gel/Gel films for leather artifact preservation. The synthesized CA-Gel complex had a total phenolic content of 139.62 ± 1.
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