Article
Food Science & Technology
Yuying Wang, Xufei Chen, Xianbing Xu, Ming Du, Beiwei Zhu, Chao Wu
Summary: In this study, a facile strategy was proposed to improve the bioavailability of curcumin by encapsulating it with unfolded soy protein. The encapsulation process formed soluble composite nano-architectures, which enhanced the solubility and stability of curcumin. The study also revealed that the interaction between curcumin and soy protein was mainly driven by hydrophobic interaction.
INNOVATIVE FOOD SCIENCE & EMERGING TECHNOLOGIES
(2022)
Article
Food Science & Technology
Bowen Zou, Xiaohan Zheng, Xianbing Xu, Xiaokang Na, Ming Du, Chao Wu
Summary: The unfolding of 11S globulin induced by reducing disulfide bonds can lead to the formation of nanoparticles, which serve as effective nanocarriers for curcumin. The exposed hydrophobic regions of the unfolded 11S globulin trigger the hydrophobic interaction between the protein and curcumin. As a result, up to 98.77% of curcumin can be encapsulated into the 11S globulin nanoparticles, forming a complex with enhanced thermal stability and water solubility.
Article
Biochemistry & Molecular Biology
Donatella Diana, Rossella Di Stasi, Sara Garcia-Vinuales, Lucia De Rosa, Carla Isernia, Gaetano Malgieri, Danilo Milardi, Luca D. D'Andrea, Roberto Fattorusso
Summary: Thermal unfolding studies provide a useful tool for understanding the conformational transitions in protein folding, with the key role of disulfide bonds in driving the folding process highlighted in this research.
Article
Biology
Oliviero Carugo
Summary: This study comprehensively analyzed the features of disulfide bonds (DBs) that bridge two protein chains in the Protein Data Bank, resulting in a structural atlas of intermolecular DBs. It was found that these DBs tend to occur between protein chains with different sequences but belonging to the same structural class. Intermolecular DBs are more solvent accessible and less distorted compared to intramolecular DBs, while showing similar B-factors. They are mainly found in beta strands and predominantly beta structures. These findings are valuable for protein modeling and design.
Article
Biochemistry & Molecular Biology
Mariana H. Moreira, Fabio C. L. Almeida, Tatiana Domitrovic, Fernando L. Palhano
Summary: Defensins are small, amphipathic proteins with disulfide bonds, challenging tertiary protein structure predictors. Comparing defensins with non-defensins showed no differences in residue proportions and solvent exposure. Bonded small proteins had more exposed apolar residues than unbonded proteins, with Robetta predicting unbonded proteins more accurately. trRosetta, using AI, improved prediction for bonded proteins but not unbonded ones, highlighting the complexity of predicting protein tertiary structures.
COMPUTATIONAL AND STRUCTURAL BIOTECHNOLOGY JOURNAL
(2021)
Article
Biochemistry & Molecular Biology
Andras Czajlik, Agnes Batta, Kinga Kerner, Adam Fizil, Dorottya Hajdu, Maria Raics, Katalin E. Kover, Gyula Batta
Summary: PAF and related antifungal proteins are stable and promising antimicrobial agents. Chemical unfolding induced by DMSO affects their folded structures but is reversible. Both NMR and DSC studies reveal the stability and unfolding behavior of PAF and its variant in DMSO/H2O mixtures, showing enhanced dynamics and fluctuation in solution.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2023)
Article
Biochemistry & Molecular Biology
Mirva J. Saaranen, Heli Alanen, Kirsi E. H. Salo, Emmanuel Nji, Pekka Karkkainen, Constanze Schmotz, Lloyd W. Ruddock
Summary: Proteins in the thioredoxin superfamily, such as protein disulfide isomerase (PDI) and glutaredoxins, have similar structures and catalytic mechanisms. PDI uses glutathione for oxidation/reduction in vitro, while glutaredoxins have a high affinity for glutathione. Mutating the active site of PDI to a more glutaredoxin-like motif increases its reactivity with glutathione.
Review
Biochemistry & Molecular Biology
Gideon Ong, Susan E. Logue
Summary: Oxidative stress is caused by an imbalance in cellular redox state due to the accumulation of reactive oxygen species (ROS). It can lead to negative effects such as damage to biological macromolecules and disruption of organelle function. The unfolded protein response (UPR), a stress response initiated by cells to combat endoplasmic reticulum (ER) stress, is well characterized, but its response and influence on oxidative stress are less defined. This review evaluates the interplay between oxidative stress, ER stress, and UPR signaling networks, particularly focusing on how UPR signaling mediators can influence antioxidant responses.
Review
Pharmacology & Pharmacy
Xulin Xu, Joyce Chiu, Shuai Chen, Chao Fang
Summary: PDI, a prototypic member of the thiol isomerase family, plays crucial roles not only in the endoplasmic reticulum but also on the cell surface and in the extracellular matrix. The in-depth study of the pathophysiological roles and molecular mechanisms of surface and extracellular PDI contributes to a better understanding of the molecular etiology of diseases.
BRITISH JOURNAL OF PHARMACOLOGY
(2021)
Review
Biochemistry & Molecular Biology
Carlos Santos-Martin, Geqing Wang, Pramod Subedi, Lilian Hor, Makrina Totsika, Jason John Paxman, Begona Heras
Summary: The DsbA enzyme, as part of the disulfide bond forming system, plays a crucial role in bacterial virulence factor assembly and is a potential target for new virulence blockers. Despite extensive studies on DSB systems in various bacterial species, little is known about how DsbA oxidoreductases recognize and interact with a wide range of substrates.
COMPUTATIONAL AND STRUCTURAL BIOTECHNOLOGY JOURNAL
(2021)
Review
Veterinary Sciences
Chunhao Han, Yifan Chen, Lei Shi, Hui Chen, Lanhui Li, Zhonghua Ning, Dan Zeng, Dehe Wang
Summary: Eggshell membranes are mainly composed of proteins, lipids, sugars, and minerals. Their special physical structure and chemical composition make them difficult to dissolve and limit their development and use. This paper reviews the latest research on separating and solubilizing eggshell membranes to provide guidance for their rational development and use.
FRONTIERS IN VETERINARY SCIENCE
(2023)
Article
Biochemical Research Methods
Timon Wittenstein, Nava Leibovich, Andreas Hilfinger
Summary: This study introduces a novel inference method that combines statistical models and mechanistic models to predict biochemical reaction rates. The method utilizes partial knowledge of network interactions and high precision probability distributions, without requiring perturbations, temporal information, or complete model knowledge. The proposed method has significant implications for quantifying complex interaction networks in cellular processes.
PLOS COMPUTATIONAL BIOLOGY
(2022)
Article
Biophysics
Yuying Wang, Xufei Chen, Xianbing Xu, Ming Du, Chao Wu
Summary: A novel method was developed to encapsulate hydrophobic compounds using self-assembly of cod protein (CP) triggered by breaking disulfide bonds. Curcumin (Cur) was used as a model to evaluate the potential of CP nanoparticles as nanocarriers. The encapsulation efficiency (EE) of CP-Cur nanoparticles was relatively high, reaching up to 99.09%, 98.8%, and 89.77% at different mass ratios of CP to Cur. The hydrophobic interaction played a crucial role in the formation of CP-Cur nanoparticles, which exhibited increased stability and a homogeneous-stable structural phase.
COLLOIDS AND SURFACES B-BIOINTERFACES
(2023)
Article
Biophysics
Veronika Dzupponova, Gabriel Zoldak
Summary: In this study, we investigated the aggregation mechanism and structures of pathological human multiple myeloma light chain aggregates (hLC) after disrupting stabilizing disulfide bonds using various reducing agents. We found that the aggregation kinetics can be described by two macroscopic rate constants related to nucleation and growth. Surprisingly, the growth rate constants decreased at higher protein concentrations due to the involvement of an aggregation active monomer particle that is successively depleted. Seeding experiments demonstrated the specificity of the aggregates and three-dimensional visualization showed variable, reducer-specific branched morphologies.
COLLOIDS AND SURFACES B-BIOINTERFACES
(2023)
Article
Chemistry, Analytical
Xiaofang Wang, Huiming Wang, Meining Zhang
Summary: Disulfide bonds are widely present in channel proteins and play vital roles in matter exchange and signal transduction. Research on disulfide bonds in nanochannels is important for understanding their biological functions. An innovative biologically-inspired artificial nanochannel based on disulfide bonds with durability and adjustable properties has been proposed. This biomimetic nanochannel shows great potential in biosensors and intelligent response designs. The study also sheds new light on channel proteins based on disulfide bonds and their modulation by environmental changes, which may contribute to the understanding of certain diseases.
Article
Chemistry, Multidisciplinary
Josep Relat-Goberna, Amy E. M. Beedle, Sergi Garcia-Manyes
Article
Biochemistry & Molecular Biology
Stefano Pernigo, Atsushi Fukuzawa, Amy E. M. Beedle, Mark Holt, Adam Round, Alessandro Pandini, Sergi Garcia-Manyes, Mathias Gautel, Roberto A. Steiner
Article
Multidisciplinary Sciences
Amy E. M. Beedle, Marc Mora, Steven Lynham, Guillaume Stirnemann, Sergi Garcia-Manyes
NATURE COMMUNICATIONS
(2017)
Review
Chemistry, Multidisciplinary
Sergi Garcia-Manyes, Amy E. M. Beedle
NATURE REVIEWS CHEMISTRY
(2017)
Article
Chemistry, Physical
Yong Jian Wang, Palma Rico-Lastres, Ainhoa Lezamiz, Marc Mora, Caries Solsona, Guillaume Stirnemann, Sergi Garcia-Manyes
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
(2018)
Article
Multidisciplinary Sciences
Judit Perales-Calvo, David Giganti, Guillaume Stirnemann, Sergi Garcia-Manyes
Article
Multidisciplinary Sciences
Amy E. M. Beedle, Marc Mora, Colin T. Davis, Ambrosius P. Snijders, Guillaume Stirnemann, Sergi Garcia-Manyes
NATURE COMMUNICATIONS
(2018)
Article
Chemistry, Multidisciplinary
Andrew Stannard, Marc Mora, Amy E. M. Beedle, Marta Castro-Lopez, Stephanie Board, Sergi Garcia-Manyes
Summary: Molecular fluctuations reveal the energy landscape of proteins, with variance analysis showing that unfolding and refolding transitions in proteins under mechanical forces result in changes in protein stiffness. The study demonstrates that the change in protein compliance with force-induced thermodynamically stable states is proportional to the protein's contour length increment, in line with the freely jointed chain model in polymer physics. These findings provide insights into the conformational dynamics of proteins under mechanical force which are crucial for mechanosensing and mechanotransduction.
Article
Chemistry, Multidisciplinary
Marc Mora, Stephanie Board, Olivier Languin-Cattoen, Laura Masino, Guillaume Stirnemann, Sergi Garcia-Manyes
Summary: Non-native disulfide bonds are dynamic covalent bridges formed in proteins, which can be detected using mechanical force and are associated with protein function and aggregation diseases.
Article
Engineering, Biomedical
Ion Andreu, Ignasi Granero-Moya, Sergi Garcia-Manyes, Pere Roca-Cusachs
Summary: Cell nuclei are affected by mechanical forces, especially through the mechanical regulation of nucleocytoplasmic transport mediated by nuclear pore complexes. Mechanical forces can increase the permeability of nuclear pore complexes by exerting force on the nucleus, and the mechanical properties of transported proteins can also regulate the rate of nucleocytoplasmic transport.
APL BIOENGINEERING
(2022)
Review
Nanoscience & Nanotechnology
Amy E. M. Beedle, Sergi Garcia-Manyes
Summary: This review discusses single-molecule force spectroscopy experiments conducted on proteins involved in mechanosensing and mechanotransduction in eukaryotic cells. Mechanical forces are emerging as a major regulator of human physiology. Single-molecule nanomechanical techniques have allowed us to gain comprehensive knowledge of the physicochemical principles governing the elasticity of single proteins and its role in mechanosensing and mechanotransduction.
NATURE REVIEWS MATERIALS
(2023)
Article
Physics, Multidisciplinary
Rafael Tapia-Rojo, Marc Mora, Stephanie Board, Jane Walker, Rajaa Boujemaa-Paterski, Ohad Medalia, Sergi Garcia-Manyes
Summary: By using single-molecule magnetic tweezers, researchers have observed previously inaccessible rare conformations of the talin protein and investigated its folding dynamics over extended periods of time. This study sheds light on the complex landscapes of protein folding and highlights the importance of observation timescale in understanding equilibrium dynamics.
Article
Multidisciplinary Sciences
Florian Franz, Rafael Tapia-Rojo, Sabina Winograd-Katz, Rajaa Boujemaa-Paterski, Wenhong Li, Tamar Unger, Shira Albeck, Camilo Aponte-Santamaria, Sergi Garcia-Manyes, Ohad Medalia, Benjamin Geiger, Frauke Graeter
Summary: This study reveals that talin activates vinculin through an intricate allosteric mechanism regulated by force. The interaction between vinculin and talin plays a crucial role in mechanosensing in cells.
NATURE COMMUNICATIONS
(2023)
Review
Chemistry, Multidisciplinary
Marc Mora, Andrew Stannard, Sergi Garcia-Manyes
CHEMICAL SOCIETY REVIEWS
(2020)
Article
Biochemistry & Molecular Biology
Alberto Elosegui-Artola, Ion Andreu, Amy E. M. Beedle, Ainhoa Lezamiz, Marina Uroz, Anita J. Kosmalska, Roger Oria, Jenny Z. Kechagia, Palma Rico-Lastres, Anabel-Lise Le Roux, Catherine M. Shanahan, Xavier Trepat, Daniel Navajas, Sergi Garcia-Manyes, Pere Roca-Cusachs