Results 11 to 20 of about 6,595 (270)

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology [PDF]

Chemical Society Reviews, 2017
Self-assembled peptide and protein amyloid nanostructures have traditionally been considered only as pathological aggregates implicated in human neurodegenerative diseases. In more recent times, these nanostructures have found interesting applications as
Arosio, Paolo, Gazit, Ehud, Hamley, Ian W., Mezzenga, Raffaele, Reynolds, Nicholas P., Su, Zhiqiang, Wei, Gang   +6 more
core   +3 more sources

The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid [PDF]

Advanced Science
Amyloids, once viewed solely as pathological hallmarks, are now recognized as widespread and versatile functional protein assemblies. Bacterial functional amyloids (FuBAs), particularly curli (CsgA) from Escherichia coli and FapC from Pseudomonas, have ...
Samuel Peña‐Díaz, Yanting Jiang, Zhefei Zhang, Anders Daugberg, Pedro Ferreira, Marcos López Hernández, Chandrika Mittal, Maria Joao Ramos, Jan Skov Pedersen, Morten Kam Dahl Dueholm, Cao Qin, Huabing Wang, Daniel E. Otzen   +12 more
doaj   +2 more sources

Biofilm-associated proteins: from the gut biofilms to neurodegeneration [PDF]

Gut Microbes
Human microbiota form a biofilm with substantial consequences for health and disease. Numerous studies have indicated that microbial communities produce functional amyloids as part of their biofilm extracellular scaffolds.
Jaione Valle
doaj   +2 more sources

Serrapeptase Eliminates Escherichia coli Biofilms by Targeting Curli Fibers, Lipopolysaccharides, and Phosphate Metabolism [PDF]

Microorganisms
Escherichia coli biofilms are implicated in the development of persistent infections and increased antibiotic resistance, posing a significant challenge in clinical settings.
Georgios Katsipis, Michalis Aivaliotis, Anastasia A. Pantazaki   +2 more
doaj   +2 more sources

Bacterial functional amyloids: Order from disorder

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2019
The discovery of intrinsic disorderness in proteins and peptide regions has given a new and useful insight into the working of biological systems. Due to enormous plasticity and heterogeneity, intrinsically disordered proteins or regions in proteins can perform myriad of functions.
Neha, Jain, Matthew R, Chapman
openaire   +5 more sources

Bacterial biofilm functionalization through Bap amyloid engineering

npj Biofilms and Microbiomes, 2022
Biofilm engineering has emerged as a controllable way to fabricate living structures with programmable functionalities. The amyloidogenic proteins comprising the biofilms can be engineered to create self-assembling extracellular functionalized surfaces ...
Leticia Matilla-Cuenca, Agustina Taglialegna, Carmen Gil, Alejandro Toledo-Arana, Iñigo Lasa, Jaione Valle   +5 more
doaj   +5 more sources

The Role of Functional Amyloids in Bacterial Virulence

Journal of Molecular Biology, 2018
Amyloid fibrils are best known as a product of human and animal protein misfolding disorders, where amyloid formation is associated with cytotoxicity and disease. It is now evident that for some proteins, the amyloid state constitutes the native structure and serves a functional role.
Van Gerven, Nani, Van der Verren, Sander E., Reiter, Dirk M., Remaut, Han   +3 more
openaire   +5 more sources

Surpassing protein specificity in biomimetics of bacterial amyloids

International Journal of Biological Macromolecules
In nature, nontoxic protein amyloids serve as dynamic, protein-specific depots, exemplified by both bacterial inclusion bodies and secretory granules from the endocrine system. Inspired by these systems, chemically defined and regulatory-compliant artificial protein microgranules have been developed for clinical applications as endocrine-like protein ...
Sanchez, Julieta Maria, Voltà Durán, Eric, Parladé Molist, Eloi, Mangues, Ramón, Villaverde Corrales, Antonio, Vazquez Gómez, Esther, Unzueta, Ugutz   +6 more
openaire   +6 more sources

Bacterial inclusion bodies are industrially exploitable amyloids

FEMS Microbiology Reviews, 2019
Understanding the structure, functionalities and biology of functional amyloids is an issue of emerging interest. Inclusion bodies, namely protein clusters formed in recombinant bacteria during protein production processes, have emerged as unanticipated, highly tunable models for the scrutiny of the physiology and architecture of functional amyloids ...
de Marco, Ario, Ferrer-Miralles, Neus, Garcia-Fruitos, Elena, Mitraki, Anna, Peternel, Spela, Rinas, Ursula, Trujillo-Roldán, Mauricio A., Valdez-Cruz, Norma A., Vázquez Gómez, Esther, Villaverde Corrales, Antonio, Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia   +10 more
exaly   +8 more sources

Bacterial Extracellular DNA Promotes β-Amyloid Aggregation [PDF]

Microorganisms, 2021
Alzheimer’s disease is associated with prion-like aggregation of the amyloid β (Aβ) peptide and the subsequent accumulation of misfolded neurotoxic aggregates in the brain. Therefore, it is critical to clearly identify the factors that trigger the cascade of Aβ misfolding and aggregation.
George Tetz, Victor Tetz
openaire   +3 more sources