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913 Results Found

  • Feature Paper
  • Article
  • Open Access
10 Citations
4,391 Views
9 Pages

4 December 2020

The polypeptide backbone of proteins is held together by two main types of covalent bonds: the peptide bonds that link the amino acid residues and the disulfide bonds that link pairs of cysteine amino acids. Disulfide bonds form as a protein folds in...

  • Article
  • Open Access
2,776 Views
22 Pages

Validation of the Intermolecular Disulfide Bond in Caspase-2

  • Megan E. Amason,
  • Lupeng Li,
  • Carissa K. Harvest,
  • Carolyn A. Lacey and
  • Edward A. Miao

17 January 2024

Caspases are a family of proteins involved in cell death. Although several caspase members have been well characterized, caspase-2 remains enigmatic. Caspase-2 has been implicated in several phenotypes, but there has been no consensus in the field ab...

  • Review
  • Open Access
62 Citations
25,542 Views
15 Pages

Cellular Disulfide Bond Formation in Bioactive Peptides and Proteins

  • Nitin A. Patil,
  • Julien Tailhades,
  • Richard Anthony Hughes,
  • Frances Separovic,
  • John D. Wade and
  • Mohammed Akhter Hossain

14 January 2015

Bioactive peptides play important roles in metabolic regulation and modulation and many are used as therapeutics. These peptides often possess disulfide bonds, which are important for their structure, function and stability. A systematic network of...

  • Review
  • Open Access
77 Citations
11,204 Views
19 Pages

31 December 2020

Disulfide bonds play a pivotal role in maintaining the natural structures of proteins to ensure their performance of normal biological functions. Moreover, biological molecular assembly, such as the gluten network, is also largely dependent on the in...

  • Review
  • Open Access
27 Citations
7,205 Views
19 Pages

16 November 2020

Oxidative protein folding involves the formation of disulfide bonds and the regeneration of native structure (N) from the fully reduced and unfolded protein (R). Oxidative protein folding studies have provided a wealth of information on underlying ph...

  • Article
  • Open Access
1,594 Views
22 Pages

23 October 2024

Background: Neurodegenerative diseases can cause vision loss by damaging retinal ganglion cells in the optic nerve. Novel phosphine-borane compounds (PBs) can protect these cells from oxidative stress via the reduction of disulfide bonds. However, th...

  • Article
  • Open Access
15 Citations
3,514 Views
20 Pages

16 January 2023

Wheat, maize, cassava, mung bean and sweet potato starches have often been added to dough systems to improve their hardness. However, inconsistent effects of these starches on the dough quality have been reported, especially in refrigerated dough. Th...

  • Article
  • Open Access
36 Citations
13,309 Views
11 Pages

Stabilization of the Single-Chain Fragment Variable by an Interdomain Disulfide Bond and Its Effect on Antibody Affinity

  • Jian-Xin Zhao,
  • Lian Yang,
  • Zhen-Nan Gu,
  • Hai-Qin Chen,
  • Feng-Wei Tian,
  • Yong-Quan Chen,
  • Hao Zhang and
  • Wei Chen

23 December 2010

The interdomain instability of single-chain fragment variable (scFv) might result in intermolecular aggregation and loss of function. In the present study, we stabilized H4—an anti-aflatoxin B1 (AFB1) scFv—with an interdomain disulfide bond and studi...

  • Article
  • Open Access
1 Citations
2,656 Views
11 Pages

Disulfide Bond Engineering of Soluble ACE2 for Thermal Stability Enhancement

  • Yoon Soo Kim,
  • Myeongbin Kim,
  • Hye Min Park,
  • Hyun Jin Kim and
  • Seong Eon Ryu

14 September 2024

Although the primary pandemic of SARS-CoV-2 is over, there are concerns about the resurgence of the next wave of related viruses, including a wide range of variant viruses. The soluble ACE2 (sACE2) inhibits the SARS-CoV-2 spike protein ACE2 interacti...

  • Article
  • Open Access
8 Citations
5,232 Views
10 Pages

Effects of an Interchain Disulfide Bond on Tropomyosin Structure: A Molecular Dynamics Study

  • Natalia A. Koubassova,
  • Sergey Y. Bershitsky and
  • Andrey K. Tsaturyan

28 October 2018

Tropomyosin (Tpm) is a coiled-coil actin-binding dimer protein that participates in the regulation of muscle contraction. Both Tpm chains contain Cys190 residues which are normally in the reduced state, but form an interchain disulfide bond in failin...

  • Article
  • Open Access
3 Citations
1,139 Views
14 Pages

3 April 2025

Interpenetrating polymer networks (IPNs) are widely used as damping materials across various industries. However, they are susceptible to issues such as microcracking or fracture over long-term service periods. To address these challenges and improve...

  • Article
  • Open Access
6 Citations
3,652 Views
11 Pages

Cysteine [2,4] Disulfide Bond as a New Modifiable Site of α-Conotoxin TxIB

  • Baojian Zhang,
  • Maomao Ren,
  • Yang Xiong,
  • Haonan Li,
  • Yong Wu,
  • Ying Fu,
  • Dongting Zhangsun,
  • Shuai Dong and
  • Sulan Luo

22 February 2021

α-Conotoxin TxIB, a selective antagonist of α6/α3β2β3 nicotinic acetylcholine receptor, could be a potential therapeutic agent for addiction and Parkinson’s disease. As a peptide with a complex pharmacophoric conformation, it is important and difficu...

  • Article
  • Open Access
21 Citations
4,484 Views
14 Pages

21 April 2022

Maltooligosaccharides are a novel type of functional oligosaccharides with potential applications in food processing and can be produced by glycosyl hydrolases hydrolyzing starch. However, the main obstacle in industrial applications is the balance b...

  • Article
  • Open Access
16 Citations
10,013 Views
18 Pages

5 August 2020

Antibodies have been used for basic research, clinical diagnostics, and therapeutic applications. Escherichia coli is one of the organisms of choice for the production of recombinant antibodies. Variable antibody genes have canonical and non-canonica...

  • Article
  • Open Access
8 Citations
8,365 Views
17 Pages

Heterogeneity in Disulfide Bond Reduction in IgG1 Antibodies Is Governed by Solvent Accessibility of the Cysteines

  • Ramakrishnan Natesan,
  • Andrew B. Dykstra,
  • Akash Banerjee and
  • Neeraj J. Agrawal

13 December 2023

We studied unpaired cysteine levels and disulfide bond susceptibility in four different γ-immunoglobulin antibodies using liquid chromatography–mass spectrometry. Our choice of differential alkylating agents ensures that the differential...

  • Article
  • Open Access
4 Citations
4,153 Views
10 Pages

Protein design is able to create artificial proteins with advanced functions, and computer simulation plays a key role in guiding the rational design. In the absence of structural evidence for cytoglobin (Cgb) with an intramolecular disulfide bond, w...

  • Article
  • Open Access
56 Citations
7,238 Views
12 Pages

31 August 2021

A self-healing waterborne polyurethane (WPU) materials containing dynamic disulfide (SS) bond was prepared by introducing SS bond into polymer materials. The zeta potential revealed that all the synthesized WPU emulsions displayed excellent stability...

  • Article
  • Open Access
1 Citations
2,430 Views
14 Pages

Stapling Cysteine[2,4] Disulfide Bond of α-Conotoxin LsIA and Its Potential in Target Delivery

  • Xin Sun,
  • Jiangnan Hu,
  • Maomao Ren,
  • Hong Chang,
  • Dongting Zhangsun,
  • Baojian Zhang and
  • Shuai Dong

14 July 2024

α-Conotoxins, as selective nAChR antagonists, can be valuable tools for targeted drug delivery and fluorescent labeling, while conotoxin-drug or conotoxin-fluorescent conjugates through the disulfide bond are rarely reported. Herein, we demonst...

  • Article
  • Open Access
5 Citations
7,171 Views
14 Pages

15 December 2014

Thioredoxin (Trx) is a small 12-kDa redox protein that catalyzes the reduction of disulfide bonds in proteins from different biological systems. A recent study of the crystal structure of white leg shrimp thioredoxin 1 from Litopenaeus vannamei (LvTr...

  • Article
  • Open Access
8 Citations
5,880 Views
17 Pages

Oxidation of Human Copper Chaperone Atox1 and Disulfide Bond Cleavage by Cisplatin and Glutathione

  • Maria I. Nardella,
  • Antonio Rosato,
  • Benny D. Belviso,
  • Rocco Caliandro,
  • Giovanni Natile and
  • Fabio Arnesano

6 September 2019

Cancer cells cope with high oxidative stress levels, characterized by a shift toward the oxidized form (GSSG) of glutathione (GSH) in the redox couple GSSG/2GSH. Under these conditions, the cytosolic copper chaperone Atox1, which delivers Cu(I) to th...

  • Article
  • Open Access
50 Citations
7,050 Views
14 Pages

Disulfide Bond Engineering of an Endoglucanase from Penicillium verruculosum to Improve Its Thermostability

  • Anna Bashirova,
  • Subrata Pramanik,
  • Pavel Volkov,
  • Aleksandra Rozhkova,
  • Vitaly Nemashkalov,
  • Ivan Zorov,
  • Alexander Gusakov,
  • Arkady Sinitsyn,
  • Ulrich Schwaneberg and
  • Mehdi D. Davari

Endoglucanases (EGLs) are important components of multienzyme cocktails used in the production of a wide variety of fine and bulk chemicals from lignocellulosic feedstocks. However, a low thermostability and the loss of catalytic performance of EGLs...

  • Article
  • Open Access
7 Citations
2,741 Views
13 Pages

26 September 2022

Mining of Phospholipase D (PLD) with high activity and stability has attracted strong interest for investigation. A novel PLD from marine Moritella sp. JT01 (MsPLD) was biochemically and structurally characterized in our previous study; however, the...

  • Communication
  • Open Access
15 Citations
4,974 Views
10 Pages

Development of a Library of Disulfide Bond-Containing Cationic Lipids for mRNA Delivery

  • Zhigao Shen,
  • Cong Liu,
  • Ziqian Wang,
  • Fengfei Xie,
  • Xingwu Liu,
  • Lingkai Dong,
  • Xuehua Pan,
  • Chen Zeng and
  • Peng George Wang

Lipid nanoparticles (LNPs) are the commonly used delivery tools for messenger RNA (mRNA) therapy and play an indispensable role in the success of COVID-19 mRNA vaccines. Ionizable cationic lipids are the most important component in LNPs. Herein, we d...

  • Article
  • Open Access
9 Citations
3,460 Views
20 Pages

4 September 2024

The complex structure of monoclonal antibodies (mAbs) expressed in Chinese hamster ovary (CHO) cells may result in the accumulation of unfolded proteins, triggering endoplasmic reticulum (ER) stress and an unfolded protein response (UPR). If the prot...

  • Article
  • Open Access
2 Citations
3,600 Views
14 Pages

16 May 2024

Every year, a significant amount of pepper stalks are wasted due to low utilization. The ash produced from pepper stalks contains a significant amount of alkaline salts, which are food additives that can enhance the quality of noodles. Therefore, uti...

  • Article
  • Open Access
4 Citations
3,076 Views
14 Pages

Evidence of RedOX Imbalance during Zika Virus Infection Promoting the Formation of Disulfide-Bond-Dependent Oligomers of the Envelope Protein

  • Grégorie Lebeau,
  • Jonathan Turpin,
  • Etienne Frumence,
  • Daed El Safadi,
  • Wissal Harrabi,
  • Philippe Desprès,
  • Pascale Krejbich-Trotot and
  • Wildriss Viranaïcken

24 May 2022

Flaviviruses replicate in membrane factories associated with the endoplasmic reticulum (ER). Significant levels of flavivirus viral protein accumulation contribute to ER stress. As a consequence, the host cell exhibits an Unfolded Protein Response (U...

  • Article
  • Open Access
27 Citations
4,431 Views
21 Pages

β-cyclodextrin(βCD)-based star polymers have attracted much interest because of their unique structures and potential biomedical and biological applications. Herein, a well-defined folic acid (FA)-conjugated and disulfide bond-linked star p...

  • Article
  • Open Access
9 Citations
11,645 Views
14 Pages

Amino Acid Patterns around Disulfide Bonds

  • José R. F. Marques,
  • Rute R. da Fonseca,
  • Brett Drury and
  • André Melo

18 November 2010

Disulfide bonds provide an inexhaustible source of information on molecular evolution and biological specificity. In this work, we described the amino acid composition around disulfide bonds in a set of disulfide-rich proteins using appropriate descr...

  • Article
  • Open Access
4 Citations
1,606 Views
11 Pages

An Orthogonal Protection Strategy for the Synthesis of Conotoxins Containing Three Disulfide Bonds

  • Hengyu Zhang,
  • Lai Yue Chan,
  • Huanhuan Zhang,
  • Tao Jiang,
  • David J. Craik,
  • Wenqing Cai and
  • Rilei Yu

14 April 2025

Disulfide bonds are crucial for stabilizing bioactive peptides such as conotoxins. We have developed a method for synthesizing conotoxins with three disulfide bonds using Mob, Trt, and Acm protection groups for regionally selective synthesis. This ap...

  • Article
  • Open Access
12 Citations
3,594 Views
11 Pages

8 October 2023

The fabrication of mechanically robust and self-healing polymeric materials remains a formidable challenge. To address the drawbacks, a core strategy is proposed based on the dynamic hard domains formed by hierarchical hydrogen bonds and disulfide bo...

  • Article
  • Open Access
12 Citations
6,755 Views
9 Pages

The Role of Individual Disulfide Bonds of μ-Conotoxin GIIIA in the Inhibition of NaV1.4

  • Penggang Han,
  • Kang Wang,
  • Xiandong Dai,
  • Ying Cao,
  • Shangyi Liu,
  • Hui Jiang,
  • Chongxu Fan,
  • Wenjian Wu and
  • Jisheng Chen

18 November 2016

μ-Conotoxin GIIIA, a peptide toxin isolated from Conus geographus, preferentially blocks the skeletal muscle sodium channel NaV1.4. GIIIA folds compactly to a pyramidal structure stabilized by three disulfide bonds. To assess the contributions of ind...

  • Article
  • Open Access
6 Citations
4,698 Views
14 Pages

Monitoring the Disulfide Bonds of Folding Isomers of Synthetic CTX A3 Polypeptide Using MS-Based Technology

  • Sheng-Yu Huang,
  • Tin-Yu Wei,
  • Bing-Shin Liu,
  • Min-Han Lin,
  • Sheng-Kuo Chiang,
  • Sung-Fang Chen and
  • Wang-Chou Sung

17 January 2019

Native disulfide formation is crucial to the process of disulfide-rich protein folding in vitro. As such, analysis of the disulfide bonds can be used to track the process of the folding reaction; however, the diverse structural isomers interfere with...

  • Review
  • Open Access
6 Citations
5,113 Views
25 Pages

Hidden Relationships between N-Glycosylation and Disulfide Bonds in Individual Proteins

  • Tania Bakshi,
  • David Pham,
  • Raminderjeet Kaur and
  • Bingyun Sun

N-Glycosylation (NG) and disulfide bonds (DBs) are two prevalent co/post-translational modifications (PTMs) that are often conserved and coexist in membrane and secreted proteins involved in a large number of diseases. Both in the past and in recent...

  • Article
  • Open Access
8 Citations
3,073 Views
14 Pages

11 December 2024

Self-healing optically transparent polyimides have potential applications in optoelectronic device fabrication. In this study, for the first time, we successfully prepared a novel self-healing polyimide film containing reversible disulfide bonds thro...

  • Article
  • Open Access
26 Citations
4,143 Views
14 Pages

Role of Disulfide Bonds and Sulfhydryl Blocked by N-Ethylmaleimide on the Properties of Different Protein-Stabilized Emulsions

  • Mangang Wu,
  • Zhikun Li,
  • Ranran Wei,
  • Yi Luan,
  • Juan Hu,
  • Qingling Wang,
  • Rui Liu,
  • Qingfeng Ge and
  • Hai Yu

10 December 2021

To investigate the role of sulfhydryl groups and disulfide bonds in different protein-stabilized emulsions, N-ethylmaleimide (NEM) was used as a sulfhydryl-blocking agent added in the emulsion. The addition of NEM to block the sulfhydryl groups resul...

  • Article
  • Open Access
25 Views
17 Pages

Structural and Catalytic Roles of the Disulfide Bonds Cys19–Cys154 and Cys134–Cys199 in Trypsin-like Proteases: Evolutionary Insights for Disulfide Bond Acquisition

  • Maiko Minakata,
  • Yuri Murakami,
  • Orika Ashida,
  • Miki Matsuzaki,
  • Kairi Ogawa,
  • Nanako Saeki,
  • Shigeru Shimamoto,
  • Mitsuhiro Miyazawa,
  • Yuji Hidaka and
  • Nana Sakata

19 January 2026

Trypsin is one of the most extensively studied enzymes in biochemistry. However, little information is available on the role of the disulfide bonds to establish the correct conformation and enzyme activity during molecular evolution. To obtain this i...

  • Feature Paper
  • Review
  • Open Access
60 Citations
10,891 Views
13 Pages

29 August 2020

Disulfide bonds are an abundant feature of proteins across all domains of life that are important for structure, stability, and function. In eukaryotic cells, a major site of disulfide bond formation is the endoplasmic reticulum (ER). How cysteines c...

  • Article
  • Open Access
5 Citations
3,095 Views
16 Pages

Functional Divergence in the Affinity and Stability of Non-Canonical Cysteines and Non-Canonical Disulfide Bonds: Insights from a VHH and VNAR Study

  • Mingce Xu,
  • Zheng Zhao,
  • Penghui Deng,
  • Mengsi Sun,
  • Cookson K. C. Chiu,
  • Yujie Wu,
  • Hao Wang and
  • Yunchen Bi

11 September 2024

Single-domain antibodies, including variable domains of the heavy chains of heavy chain-only antibodies (VHHs) from camelids and variable domains of immunoglobulin new antigen receptors (VNARs) from cartilaginous fish, show the therapeutic potential...

  • Article
  • Open Access
6 Citations
3,726 Views
17 Pages

NMR-Based Structural Characterization of a Two-Disulfide-Bonded Analogue of the FXIIIa Inhibitor Tridegin: New Insights into Structure–Activity Relationships

  • Thomas Schmitz,
  • Ajay Abisheck Paul George,
  • Britta Nubbemeyer,
  • Charlotte A. Bäuml,
  • Torsten Steinmetzer,
  • Oliver Ohlenschläger,
  • Arijit Biswas and
  • Diana Imhof

The saliva of blood-sucking leeches contains a plethora of anticoagulant substances. One of these compounds derived from Haementeria ghilianii, the 66mer three-disulfide-bonded peptide tridegin, specifically inhibits the blood coagulation factor FXII...

  • Article
  • Open Access
30 Citations
10,366 Views
21 Pages

25 February 2016

One of the factors responsible for tertiary structural stabilization in proteins is the presence of the hydrophobic core—a result of hydrophobic interactions within the protein body. In some proteins (especially extracellular ones) additional stabili...

  • Article
  • Open Access
2 Citations
3,939 Views
13 Pages

Role of Disulfide Bonds in Activity and Stability of Tigerinin-1R

  • Xiaolong Chen,
  • Cuihua Hu,
  • Yibing Huang and
  • Yuxin Chen

Tigerinin-1R (Arg–Val–Cys–Ser–Ala–Ile–Pro–Leu–Pro–Ile–Cys–His–NH2), a cationic 12-mer peptide containing a disulfide bond extracted from frog skin secretions, lacks antibacterial activity, but has the ability to stimulate insulin release both in vitr...

  • Article
  • Open Access
7 Citations
2,432 Views
15 Pages

The Marine Antimicrobial Peptide AOD with Intact Disulfide Bonds Has Remarkable Antibacterial and Anti-Biofilm Activity

  • Ruoyu Mao,
  • Qingyi Zhao,
  • Haiqiang Lu,
  • Na Yang,
  • Yuanyuan Li,
  • Da Teng,
  • Ya Hao,
  • Xinxi Gu and
  • Jianhua Wang

8 October 2024

American Oyster Defensin (AOD) is a marine peptide that is derived from North American mussels. It has been demonstrated to exhibit potent antimicrobial activity and high safety in both in vitro and in vivo models. In this study, to facilitate synthe...

  • Article
  • Open Access
4 Citations
2,800 Views
13 Pages

Stabilization of Cereibacter sphaeroides Photosynthetic Reaction Center by the Introduction of Disulfide Bonds

  • Georgii Selikhanov,
  • Anastasia Atamas,
  • Diana Yukhimchuk,
  • Tatiana Fufina,
  • Lyudmila Vasilieva and
  • Azat Gabdulkhakov

25 January 2023

The photosynthetic reaction center of the purple nonsulfur bacterium Cereibacter sphaeroides is a useful model for the study of mechanisms of photoinduced electron transfer and a promising component for photo-bio-electrocatalytic systems. The basic r...

  • Article
  • Open Access
2 Citations
2,741 Views
11 Pages

30 June 2022

About 5% of the disulfide bonds (DBs) observed in the Protein Data Bank bridge two protein chains. Several of their features were comprehensively analyzed, resulting in a structural atlas of the intermolecular DBs. The analysis was performed on a ver...

  • Article
  • Open Access
1 Citations
2,241 Views
12 Pages

Design and Escherichia coli Expression of a Natively Folded Multi-Disulfide Bonded Influenza H1N1-PR8 Receptor-Binding Domain (RBD)

  • Thao Tu,
  • Tharangani Rathnayaka,
  • Toshiyo Kato,
  • Kenji Mizutani,
  • Tomonori Saotome,
  • Keiichi Noguchi,
  • Shun-ichi Kidokoro and
  • Yutaka Kuroda

Refolding multi-disulfide bonded proteins expressed in E. coli into their native structure is challenging. Nevertheless, because of its cost-effectiveness, handiness, and versatility, the E. coli expression of viral envelope proteins, such as the RBD...

  • Commentary
  • Open Access
Cancers2026, 18(2), 339;https://doi.org/10.3390/cancers18020339 
(registering DOI)

21 January 2026

Quiescin sulfhydryl oxidase 1 (QSOX1) is a disulfide bond-forming enzyme with both disulfide isomerase and oxidoreductase activities. It plays an important role in protein folding, stability, and secretion. Growing evidence demonstrates that QSOX1 is...

  • Article
  • Open Access
5 Citations
2,238 Views
17 Pages

Discovery and Visualization of the Hidden Relationships among N-Glycosylation, Disulfide Bonds, and Membrane Topology

  • Manthan Desai,
  • Amritpal Singh,
  • David Pham,
  • Syed Rafid Chowdhury and
  • Bingyun Sun

10 November 2023

Membrane proteins (MPs) are functionally important but structurally complex. In particular, MPs often carry three structural features, i.e., transmembrane domains (TMs), disulfide bonds (SSs), and N-glycosylation (N-GLYCO). All three features have be...

  • Article
  • Open Access
10 Citations
3,597 Views
12 Pages

Characterization and Utilization of Disulfide-Bonded SARS-CoV-2 Receptor Binding Domain of Spike Protein Synthesized by Wheat Germ Cell-Free Production System

  • Yutaro Yamaoka,
  • Sundararaj Stanleyraj Jeremiah,
  • Rikako Funabashi,
  • Kei Miyakawa,
  • Takeshi Morita,
  • Yusaku Mihana,
  • Hideaki Kato and
  • Akihide Ryo

1 July 2022

The spike protein (SP) of SARS-CoV-2 is an important target for COVID-19 therapeutics and vaccines as it binds to the ACE2 receptor and enables viral infection. Rapid production and functional characterization of properly folded SP is of the utmost i...

  • Article
  • Open Access
19 Citations
3,760 Views
13 Pages

Ultrasound treatment can improve enzymolysis efficiency by changing the amounts of sulfhydryl groups (SH) and disulfide bonds (SS) in protein. This paper proposes an in-situ and real-time monitoring method for SH and SS during ultrasound application...

  • Article
  • Open Access
2 Citations
1,084 Views
21 Pages

29 May 2025

In this study, an investigation on using polyurethane/graphene oxide (PU/GO) containing disulfide bonds as a modifier to improve the self-healing ability of asphalt was conducted. PU/GO with different GO contents were synthesized and modified asphalt...

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