This study presents a novel approach to harnessing the underutilized resource of livestock blood plasma proteins to produce bioplastic films based on amyloid fibrils. Upon acidic heating, a 20-h incubation period resulted in mature, semiflexible fibrils with an average length of 0.65 μm and a persistence length of 261 nm. Characterization using Thioflavin T intensity, circular dichroism, and FTIR spectroscopy revealed a cross-β-sheet structure stabilized by hydrogen bonding. The integration of plasma protein amyloid fibrils with poly(vinyl alcohol) (PVA) or methyl cellulose (MC) yielded bioplastic films that exhibit smooth and homogeneous micromorphology, enhanced toughness, and water stability, with PVA-based films demonstrating an exceptional elongation of ∼300%, suitable for food packaging applications. Compared to petroleum-based plastics, plasma amyloid fibril-incorporated films demonstrated a superior sustainability footprint (∼92%). This work underscores the potential of plasma protein amyloid fibrils in bioplastic applications, aligning with the global imperative for eco-friendly waste management and a circular economy.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/acs.biomac.4c01564 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Aggregatin is a mitochondrial regulator of MAVS activation to drive innate immunity.
J Immunol
February 2025
Department of Pharmacology and Toxicology, University of Arizona, Tucson, AZ, United States.
Mitochondrial antiviral-signaling protein (MAVS) is a key adapter protein required for inducing type I interferons (IFN-Is) and other antiviral effector molecules. The formation of MAVS aggregates on mitochondria is essential for its activation; however, the regulatory mitochondrial factor that mediates the aggregation process is unknown. Our recent work has identified the protein Aggregatin as a critical seeding factor for β-amyloid peptide aggregation.
View Article and Find Full Text PDFHigh-Throughput Proteoform Imaging for Revealing Spatial-Resolved Changes in Brain Tissues Associated with Alzheimer's Disease.
Adv Sci (Weinh)
March 2025
State Key Laboratory of Medical Proteomics, National Chromatographic R. & A. Center, CAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 457 Zhongshan Road, Dalian, 116023, China.
Spatially resolved characterization of proteoforms has substantial potential to significantly advance the understanding of physiological and disease mechanisms. However, challenges remain regarding throughput and coverage. A robust method is developed for high-throughput proteoform imaging (HTPi) by combining matrix-assisted laser desorption ionization mass spectrometry imaging (MALDI MSI) and region-specific top-down proteomic analysis.
View Article and Find Full Text PDFThe role of protein phosphorylation modifications mediated by iron metabolism regulatory networks in the pathogenesis of Alzheimer's disease.
Front Aging Neurosci
February 2025
Hospital of Encephalopathy, The First Affiliated Hospital of Henan University of Chinese Medicine, Zhengzhou, China.
Alzheimer's disease (AD) is a severe neurodegenerative disease characterized mainly by the formation of amyloid beta (Aβ) plaques and abnormal phosphorylation of tau. In recent years, an imbalance in iron homeostasis has been recognized to play a key role in the pathological process of AD. Abnormal iron accumulation can activate various kinases such as glycogen synthase kinase-3β, cyclin-dependent kinase 5, and mitogen-activated protein kinase, leading to abnormal phosphorylation of tau and amyloid precursor protein, and accelerating the formation of Aβ plaques and neurofibrillary tangles.
View Article and Find Full Text PDFReduced protein solubility - cause or consequence in amyloid disease?
QRB Discov
February 2025
Biochemistry and Structural Biology, Lund University, Lund, Sweden.
In this perspective, we ask the question whether the apparently lower solubility of specific proteins in amyloid disease is a cause or consequence of the protein deposition seen in such diseases. We focus on Alzheimer's disease and start by reviewing the experimental evidence of disease-associated reduction in the measured concentration of amyloid β peptide, Aβ42, in cerebrospinal fluid. We propose a series of possible physicochemical explanations for these observations.
View Article and Find Full Text PDFDepletion of nuclear cytoophidia in Alzheimer's disease.
Free Neuropathol
January 2025
Department of Laboratory Medicine, St. Michael's Hospital, Unity Health & Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada.
There is considerable evidence for a role for metabolic dysregulation, including disordered purine nucleotide metabolism, in the pathogenesis of Alzheimer's disease (AD). Purine nucleotide synthesis in the brain is regulated with high fidelity to co-ordinate supply with demand. The assembly of some purine biosynthetic enzymes into linear filamentous aggregates called "cytoophidia" (Gk.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!