Encapsulated essential oils in protein-polysaccharide biopolymers: characteristics and applications in the biomedical and food industries DOI
Bogale Worku, Nurelegne Tefera Shibeshi,

Tian Zhiyuan

et al.

Food Science and Biotechnology, Journal Year: 2024, Volume and Issue: 34(4), P. 851 - 869

Published: Nov. 21, 2024

Language: Английский

Engineered protein-based materials for tissue repair: A review DOI
Jiayin Feng, Fangyan Wang,

Yunyuan Shao

et al.

International Journal of Biological Macromolecules, Journal Year: 2025, Volume and Issue: 303, P. 140674 - 140674

Published: Feb. 3, 2025

Language: Английский

Citations

8

A temperature-inducible protein module for control of mammalian cell fate DOI
William Benman, Zikang Huang, Pavan Iyengar

et al.

Nature Methods, Journal Year: 2025, Volume and Issue: unknown

Published: Jan. 23, 2025

Language: Английский

Citations

2

Proteins for Hyperelastic Materials DOI Open Access

Rui Su,

Chao Ma, Bing Han

et al.

Small, Journal Year: 2025, Volume and Issue: unknown

Published: Feb. 5, 2025

Meticulous engineering and the yielded hyperelastic performance of structural proteins represent a new frontier in developing next-generation functional biomaterials. These materials exhibit outstanding programmable mechanical properties, including elasticity, resilience, toughness, active biological characteristics, such as degradability tissue repairability, compared with their chemically synthetic counterparts. However, there are several critical issues regarding preparation approaches protein-based materials: limited natural sequence modules, non-hierarchical assembly, imbalance between compressive tensile leading to unmet demands. Therefore, it is pivotal develop an alternative strategy for biofabricating materials. Herein, molecular design, engineering, property regulation overviewed. First, methodologies deeper exploration machine learning-aided de novo random mutations sequences, multiblock fusion techniques, actively introduced. facilitate generation elastomeric protein modules demonstrate enhanced versatility. Subsequently, assembly tactics (i.e., physical modulation, genetic adaptations, chemical modifications) reviewed, yielding hierarchically ordered structures. Finally, advances biophysical techniques more nuanced characterization ensembles discussed, unveiling tuning mechanisms elasticity across scales. Future developments biomaterials also envisioned.

Language: Английский

Citations

1

Precision Loading and Delivery of Molecular Cargo by Size-Controlled Coacervation of Gold Nanoparticles Functionalized with Elastin-like Peptides DOI

Yifeng Cai,

Nada Y. Naser, Jinrong Ma

et al.

Biomacromolecules, Journal Year: 2024, Volume and Issue: 25(4), P. 2390 - 2398

Published: March 13, 2024

Thermoresponsive elastin-like peptides (ELPs) have been extensively investigated in biotechnology and medicine, but little attention has paid to the process by which coacervation causes ELP-decorated particles aggregate. Using gold nanoparticles (AuNPs) functionalized with a cysteine-terminated 96-repeat of VPGVG sequence (V96-Cys), we show that size clusters reversibly form above ELP transition temperature can be finely controlled 250 930 nm range specifying concentration free V96-Cys solution using AuNPs different sizes. We further find localized surface plasmon resonance peak embedded progressively red-shifts cluster size, likely due an increase particle–particle contacts. exploit this fine control over homogeneously load precise amounts dye Nile Red antibiotic Tetracycline into hydrodynamic diameters deliver cargos near-quantitatively deconstructing aggregates below temperature. Beyond establishing key role for ELPs agglomeration ELP-functionalized particles, our results provide path thermally delivery quantities molecular cargo. This capability might prove useful combination photothermal therapies theranostic applications, trigger spatially temporally uniform responses from biological, electronic, or optical systems.

Language: Английский

Citations

6

A temperature-inducible protein module for control of mammalian cell fate DOI Creative Commons
William Benman,

Zikang Huang,

Pavan Iyengar

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: Feb. 19, 2024

Abstract Inducible protein switches allow on-demand control of proteins in response to inputs including chemicals or light. However, these either cannot be controlled with precision space and time applied optically dense settings, limiting their application tissues organisms. Here we introduce a module whose active state can reversibly toggled small change temperature, stimulus that is both penetrant dynamic. This protein, called Melt ( Me mbrane localization through temperature), exists as monomer the cytoplasm at elevated temperatures but oligomerizes translocates plasma membrane when temperature lowered. The original variant switched states between 28-32°C, changes could observed within minutes change. was highly modular, permitting thermal over diverse processes signaling, proteolysis, nuclear shuttling, cytoskeletal rearrangements, cell death, all straightforward end-to-end fusions. also tunable, giving rise library variants switch point ranging from 30-40°C. higher points allowed molecular circuits 37°C-41°C, well-tolerated range for mammalian cells. Finally, permitted death mouse model human cancer, demonstrating its potential use animals. Thus represents versatile thermogenetic straightforward, non-invasive, spatiotemporally-defined cells broad biotechnology biomedicine.

Language: Английский

Citations

4

Advances in nanobody multimerization and multispecificity: from in vivo assembly to in vitro production DOI Creative Commons

Mohammed Al‐Seragi,

Yilun Chen,

Franck Duong

et al.

Biochemical Society Transactions, Journal Year: 2025, Volume and Issue: 53(01)

Published: Feb. 7, 2025

NANOBODIES® (Nbs) have emerged as valuable tools across therapeutic, diagnostic, and industrial applications owing to their small size consequent ability bind unique epitopes inaccessible conventional antibodies. While Nbs retrieved from immune libraries normally possess sufficient affinity specificity for cognate antigens in the practical use case, multimerization will often increase functional via avidity effects. Therefore, rescue binding broaden targeting specificities, recent efforts focused on conjugating multiple Nb clones — of identical or antigen cognates together. In vivo vitro approaches, including flexible linkers, antibody domains, self-assembling coiled coils, chemical conjugation, self-clustering hydrophobic sequences, been employed produce multivalent multispecific constructs. Examples successful are diverse, ranging immunoassaying reagents virus-neutralizing moieties. This review aims recapitulate modalities while highlighting applications, advantages, drawbacks tied each method.

Language: Английский

Citations

0

Nanoenhanced‐Cuproptosis Results From the Synergy of Calcium Overload and GSH Depletion with the Increasing of Intracellular Ca/Mn/Cu Ions DOI Creative Commons

Shiwei Liu,

Wennan Yan,

Wenyue Zhang

et al.

Advanced Science, Journal Year: 2025, Volume and Issue: unknown

Published: Feb. 10, 2025

Abstract Cuproptosis is a newly discovered copper‐dependent form of cell death. Intracellular glutathione (GSH) acts as copper chelator to inhibit cuproptosis, so the reduction GSH concentration conducive enhancing cuproptosis cells. In order reduce content and interfere with mitochondrial metabolism, strategy based on calcium overload depletion enhance proposed in this study. Containing manganese (Mn) (Cu) elements, CaCO 3 nanoparticles (NPs) are modified MCF‐7 aptamer (CaCO /Mn/Cu@lip‐Apt). When entering cell, /Mn/Cu@lip‐Apt decomposed released Mn* (Mn 2+ /Mn 3+ 4+ ), Cu Ca . The high valence Mn ion can effectively consume produce which catalyzed H 2 O reactive oxygen species (ROS), while reducing concentration. production ROS promoted influx exogenous large accumulation led intracellular overload, resulting dysfunction metabolism disorders. , turn triggered cuproptosis. This showed excellent antitumor effects provided new way study disease treatment.

Language: Английский

Citations

0

Spontaneous Self‐Organized Order Emerging From Intrinsically Disordered Protein Polymers DOI Creative Commons
Sergio Acosta,

Pablo Rodríguez‐Alonso,

Viktoriya Chaskovska

et al.

Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology, Journal Year: 2025, Volume and Issue: 17(1)

Published: Jan. 1, 2025

ABSTRACT Intrinsically disordered proteins (IDPs) are that, despite lacking a defined 3D structure, capable of adopting dynamic conformations. This structural adaptability allows them to play not only essential roles in crucial cellular processes, such as subcellular organization or transcriptional control, but also coordinating the assembly macromolecules during different stages development. Thus, order artificially replicate complex processes morphogenesis and their dynamics, it is have materials that recapitulate plasticity IDPs. In this regard, intrinsically protein polymers (IDPPs) emerge promising for engineering synthetic condensates creating hierarchically self‐assembled materials. IDPPs exhibit remarkable properties use biofabrication, functional versatility, tunable sequence order–disorder, ability undergo liquid–liquid phase separation (LLPS). Recent research has focused on harnessing intrinsic disorder design architectures with tailored properties. Taking advantage stimuli‐responsiveness degree disorder, researchers developed innovative strategies control self‐assembly IDPPs, resulting creation organized structures intricate morphologies. review, we aim provide an overview latest advances application IDPP‐based materials, shedding light fundamental principles supramolecular assembly, discussing biomedical nanobiotechnological fields.

Language: Английский

Citations

0

The Internal Structural Dynamics of Elastin-Like Polypeptide Assemblies by 13C-Direct Detected NMR Spectroscopy DOI Creative Commons

Dörte Brandis,

Pavel Kadeřávek, Dennis Kurzbach

et al.

Analytical Chemistry, Journal Year: 2025, Volume and Issue: unknown

Published: Feb. 16, 2025

Elastin-like polypeptides (ELPs) are biocompatible polymers exhibiting lower critical solution temperature (LCST) behavior, making them valuable in various applications, including drug delivery and tissue engineering. This study addresses the atomistic-level understanding of ELP self-assembly, focusing on their internal structural dynamics. Conventional proton-detected nuclear magnetic resonance (NMR) spectroscopy faces limitations studying aggregates due to accelerated proton exchange processes, which cause significant broadening. Herein, we show how overcome this hurdle by using carbon-13-detected NMR. method mitigates issues related amide exchange, allowing for a residue-resolved view configuration aggregates. With method, record 15N relaxation rates, revealing three features. (i) Proline residues within PGXGV pentapeptide repeats (X being any amino acid except proline) become motional restricted upon aggregation, indicating role as interchain contacts. (ii) Pentapeptides with alanine guest residue X display particularly significantly reduced freedom aggregation. (iii) Even large aggregates, fast dynamics characterize peptide chains way that is reminiscent condensed liquid phases. The presented first proof concept 13C-direct detection viable tool delineate phases It might, thus, help foster new investigations aggregation mechanisms.

Language: Английский

Citations

0

Efficiently scaled-up production of recombinant human elastin-like polypeptides using multiple optimization strategies DOI
Jianping Xiong,

L. Liu,

Yu Wei

et al.

Journal of Biotechnology, Journal Year: 2025, Volume and Issue: unknown

Published: Feb. 1, 2025

Language: Английский

Citations

0