Log in

Relevant bibliographies by topics / Sortase-mediated ligation / Journal articles

Journal articles on the topic 'Sortase-mediated ligation'

To see the other types of publications on this topic, follow the link: Sortase-mediated ligation.

Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Sortase-mediated ligation.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Wang, Hejia Henry, Burcin Altun, Kido Nwe, and Andrew Tsourkas. "Proximity-Based Sortase-Mediated Ligation." Angewandte Chemie 129, no. 19 (April 7, 2017): 5433–36. http://dx.doi.org/10.1002/ange.201701419.

Full text

APA, Harvard, Vancouver, ISO, and other styles

2

Wang, Hejia Henry, Burcin Altun, Kido Nwe, and Andrew Tsourkas. "Proximity-Based Sortase-Mediated Ligation." Angewandte Chemie International Edition 56, no. 19 (April 4, 2017): 5349–52. http://dx.doi.org/10.1002/anie.201701419.

Full text

APA, Harvard, Vancouver, ISO, and other styles

3

Valgardson, Jordan D., Sarah A. Struyvenberg, Zachary R. Sailer, Isabel M. Piper, Justin E. Svendsen, D. Alex Johnson, Brandon A. Vogel, John M. Antos, Michael J. Harms, and Jeanine F. Amacher. "Comparative Analysis and Ancestral Sequence Reconstruction of Bacterial Sortase Family Proteins Generates Functional Ancestral Mutants with Different Sequence Specificities." Bacteria 1, no. 2 (June 9, 2022): 121–35. http://dx.doi.org/10.3390/bacteria1020011.

Full text

Abstract:

Gram-positive bacteria are some of the earliest known life forms, diverging from gram-negative bacteria 2 billion years ago. These organisms utilize sortase enzymes to attach proteins to their peptidoglycan cell wall, a structural feature that distinguishes the two types of bacteria. The transpeptidase activity of sortases make them an important tool in protein engineering applications, e.g., in sortase-mediated ligations or sortagging. However, due to relatively low catalytic efficiency, there are ongoing efforts to create better sortase variants for these uses. Here, we use bioinformatics tools, principal component analysis and ancestral sequence reconstruction, in combination with protein biochemistry, to analyze natural sequence variation in these enzymes. Principal component analysis on the sortase superfamily distinguishes previously described classes and identifies regions of relatively high sequence variation in structurally-conserved loops within each sortase family, including those near the active site. Using ancestral sequence reconstruction, we determined sequences of ancestral Staphylococcus and Streptococcus Class A sortase proteins. Enzyme assays revealed that the ancestral Streptococcus enzyme is relatively active and shares similar sequence variation with other Class A Streptococcus sortases. Taken together, we highlight how natural sequence variation can be utilized to investigate this important protein family, arguing that these and similar techniques may be used to discover or design sortases with increased catalytic efficiency and/or selectivity for sortase-mediated ligation experiments.

APA, Harvard, Vancouver, ISO, and other styles

4

Dai, Xiaolin, Diana Mate, Ulrich Glebe, Tayebeh Mirzaei Garakani, Andrea Körner, Ulrich Schwaneberg, and Alexander Böker. "Sortase-Mediated Ligation of Purely Artificial Building Blocks." Polymers 10, no. 2 (February 6, 2018): 151. http://dx.doi.org/10.3390/polym10020151.

Full text

APA, Harvard, Vancouver, ISO, and other styles

5

Han, Ying, Yifan Da, Mingjia Yu, Yaping Cheng, Xin Wang, Jiale Xiong, Guoying Guo, Yan Li, Xianxing Jiang, and Xiaoqing Cai. "Protein labeling approach to improve lysosomal targeting and efficacy of antibody–drug conjugates." Organic & Biomolecular Chemistry 18, no. 17 (2020): 3229–33. http://dx.doi.org/10.1039/d0ob00265h.

Full text

APA, Harvard, Vancouver, ISO, and other styles

6

Chen, Qi, Qing Sun, Nicholas M. Molino, Szu-Wen Wang, Eric T. Boder, and Wilfred Chen. "Sortase A-mediated multi-functionalization of protein nanoparticles." Chemical Communications 51, no. 60 (2015): 12107–10. http://dx.doi.org/10.1039/c5cc03769g.

Full text

Abstract:

A new strategy was developed to create multi-functionalizaton of protein nanoparticles using Sortase A-mediated ligation, resulting in modified protein nanoparticles that are both thermally responsive and catalytic active.

APA, Harvard, Vancouver, ISO, and other styles

7

Dai, Xiaolin, Alexander Böker, and Ulrich Glebe. "Broadening the scope of sortagging." RSC Advances 9, no. 9 (2019): 4700–4721. http://dx.doi.org/10.1039/c8ra06705h.

Full text

APA, Harvard, Vancouver, ISO, and other styles

8

Williamson, Daniel J., Michael E. Webb, and W. Bruce Turnbull. "Depsipeptide substrates for sortase-mediated N-terminal protein ligation." Nature Protocols 9, no. 2 (January 9, 2014): 253–62. http://dx.doi.org/10.1038/nprot.2014.003.

Full text

APA, Harvard, Vancouver, ISO, and other styles

9

Liu, Fa, Ethan Y. Luo, David B. Flora, and Adam R. Mezo. "Irreversible Sortase A-Mediated Ligation Driven by Diketopiperazine Formation." Journal of Organic Chemistry 79, no. 2 (January 6, 2014): 487–92. http://dx.doi.org/10.1021/jo4024914.

Full text

APA, Harvard, Vancouver, ISO, and other styles

10

Matsumoto, Takuya, Kou Furuta, Tsutomu Tanaka, and Akihiko Kondo. "Sortase A-Mediated Metabolic Enzyme Ligation in Escherichia coli." ACS Synthetic Biology 5, no. 11 (October 11, 2016): 1284–89. http://dx.doi.org/10.1021/acssynbio.6b00194.

Full text

APA, Harvard, Vancouver, ISO, and other styles

11

Mao, Hongyuan, Scott A. Hart, Amy Schink, and Brian A. Pollok. "Sortase-Mediated Protein Ligation: A New Method for Protein Engineering." Journal of the American Chemical Society 126, no. 9 (March 2004): 2670–71. http://dx.doi.org/10.1021/ja039915e.

Full text

APA, Harvard, Vancouver, ISO, and other styles

12

Jiang, Rui, Jacob Weingart, Hailong Zhang, Yong Ma, and Xue-Long Sun. "End-Point Immobilization of Recombinant Thrombomodulin via Sortase-Mediated Ligation." Bioconjugate Chemistry 23, no. 3 (March 8, 2012): 643–49. http://dx.doi.org/10.1021/bc200661w.

Full text

APA, Harvard, Vancouver, ISO, and other styles

13

Cheng, Xiaozhong, Tao Zhu, Haofei Hong, Zhifang Zhou, and Zhimeng Wu. "Sortase A-mediated on-resin peptide cleavage and in situ ligation: an efficient one-pot strategy for the synthesis of functional peptides and proteins." Organic Chemistry Frontiers 4, no. 10 (2017): 2058–62. http://dx.doi.org/10.1039/c7qo00481h.

Full text

Abstract:

A one-pot approach combining Sortase A mediated on-resin peptide cleavage, activation and in situ ligation was developed and was employed to synthesize dual functional peptides, modify peptides with lipid, biotin and PEG, as well as protein N-terminal labeling in high efficiency.

APA, Harvard, Vancouver, ISO, and other styles

14

Reed, Sierra A., David A. Brzovic, Savanna S. Takasaki, Kristina V. Boyko, and John M. Antos. "Efficient Sortase-Mediated Ligation Using a Common C-Terminal Fusion Tag." Bioconjugate Chemistry 31, no. 5 (April 23, 2020): 1463–73. http://dx.doi.org/10.1021/acs.bioconjchem.0c00156.

Full text

APA, Harvard, Vancouver, ISO, and other styles

15

Cambria, Elena, Kasper Renggli, Caroline C. Ahrens, Christi D. Cook, Carsten Kroll, Andrew T. Krueger, Barbara Imperiali, and Linda G. Griffith. "Covalent Modification of Synthetic Hydrogels with Bioactive Proteins via Sortase-Mediated Ligation." Biomacromolecules 16, no. 8 (July 10, 2015): 2316–26. http://dx.doi.org/10.1021/acs.biomac.5b00549.

Full text

APA, Harvard, Vancouver, ISO, and other styles

16

Tsukiji, Shinya, and Teruyuki Nagamune. "Sortase-Mediated Ligation: A Gift from Gram-Positive Bacteria to Protein Engineering." ChemBioChem 10, no. 5 (March 23, 2009): 787–98. http://dx.doi.org/10.1002/cbic.200800724.

Full text

APA, Harvard, Vancouver, ISO, and other styles

17

Wójcik, Magdalena, Susana Vázquez Torres, Wim J. Quax, and Ykelien L. Boersma. "Sortase mutants with improved protein thermostability and enzymatic activity obtained by consensus design." Protein Engineering, Design and Selection 32, no. 12 (December 2019): 555–64. http://dx.doi.org/10.1093/protein/gzaa018.

Full text

Abstract:

Abstract Staphylococcus aureus sortase A (SaSrtA) is an enzyme that anchors proteins to the cell surface of Gram-positive bacteria. During the transpeptidation reaction performed by SaSrtA, proteins containing an N-terminal glycine can be covalently linked to another protein with a C-terminal LPXTG motif (X being any amino acid). Since the sortase reaction can be performed in vitro as well, it has found many applications in biotechnology. Although sortase-mediated ligation has many advantages, SaSrtA is limited by its low enzymatic activity and dependence on Ca2+. In our study, we evaluated the thermodynamic stability of the SaSrtA wild type and found the enzyme to be stable. We applied consensus analysis to further improve the enzyme’s stability while at the same time enhancing the enzyme’s activity. As a result, we found thermodynamically improved, more active and Ca2+-independent mutants. We envision that these new variants can be applied in conjugation reactions in low Ca2+ environments.

APA, Harvard, Vancouver, ISO, and other styles

18

Yamamura, Yuichi, Hidehiko Hirakawa, Satoshi Yamaguchi, and Teruyuki Nagamune. "Enhancement of sortase A-mediated protein ligation by inducing a β-hairpin structure around the ligation site." Chemical Communications 47, no. 16 (2011): 4742. http://dx.doi.org/10.1039/c0cc05334a.

Full text

APA, Harvard, Vancouver, ISO, and other styles

19

Staus, Dean P., Laura M. Wingler, Minjung Choi, Biswaranjan Pani, Aashish Manglik, Andrew C. Kruse, and Robert J. Lefkowitz. "Sortase ligation enables homogeneous GPCR phosphorylation to reveal diversity in β-arrestin coupling." Proceedings of the National Academy of Sciences 115, no. 15 (March 26, 2018): 3834–39. http://dx.doi.org/10.1073/pnas.1722336115.

Full text

Abstract:

The ability of G protein-coupled receptors (GPCRs) to initiate complex cascades of cellular signaling is governed by the sequential coupling of three main transducer proteins, G protein, GPCR kinase (GRK), and β-arrestin. Mounting evidence indicates these transducers all have distinct conformational preferences and binding modes. However, interrogating each transducer’s mechanism of interaction with GPCRs has been complicated by the interplay of transducer-mediated signaling events. For example, GRK-mediated receptor phosphorylation recruits and induces conformational changes in β-arrestin, which facilitates coupling to the GPCR transmembrane core. Here we compare the allosteric interactions of G proteins and β-arrestins with GPCRs’ transmembrane cores by using the enzyme sortase to ligate a synthetic phosphorylated peptide onto the carboxyl terminus of three different receptors. Phosphopeptide ligation onto the β2-adrenergic receptor (β2AR) allows stabilization of a high-affinity receptor active state by β-arrestin1, permitting us to define elements in the β2AR and β-arrestin1 that contribute to the receptor transmembrane core interaction. Interestingly, ligation of the identical phosphopeptide onto the β2AR, the muscarinic acetylcholine receptor 2 and the μ-opioid receptor reveals that the ability of β-arrestin1 to enhance agonist binding relative to G protein differs substantially among receptors. Furthermore, strong allosteric coupling of β-arrestin1 correlates with its ability to attenuate, or “desensitize,” G protein activation in vitro. Sortase ligation thus provides a versatile method to introduce complex, defined phosphorylation patterns into GPCRs, and analogous strategies could be applied to other classes of posttranslationally modified proteins. These homogeneously phosphorylated GPCRs provide an innovative means to systematically study receptor–transducer interactions.

APA, Harvard, Vancouver, ISO, and other styles

20

Yu, Wendy, Kevin P. Gillespie, Bonirath Chhay, Anne-Sophie Svensson, Per-Åke Nygren, Ian A. Blair, Feifan Yu, and Andrew Tsourkas. "Efficient Labeling of Native Human IgG by Proximity-Based Sortase-Mediated Isopeptide Ligation." Bioconjugate Chemistry 32, no. 6 (May 24, 2021): 1058–66. http://dx.doi.org/10.1021/acs.bioconjchem.1c00099.

Full text

APA, Harvard, Vancouver, ISO, and other styles

21

Pritz, Stephan, Yvonne Wolf, Oliver Kraetke, Jana Klose, Michael Bienert, and Michael Beyermann. "Synthesis of Biologically Active Peptide Nucleic Acid−Peptide Conjugates by Sortase-Mediated Ligation." Journal of Organic Chemistry 72, no. 10 (May 2007): 3909–12. http://dx.doi.org/10.1021/jo062331l.

Full text

APA, Harvard, Vancouver, ISO, and other styles

22

Chan, Lilyan, Hannah F. Cross, Joseph K. She, Gabriel Cavalli, Hugo F. P. Martins, and Cameron Neylon. "Covalent Attachment of Proteins to Solid Supports and Surfaces via Sortase-Mediated Ligation." PLoS ONE 2, no. 11 (November 14, 2007): e1164. http://dx.doi.org/10.1371/journal.pone.0001164.

Full text

APA, Harvard, Vancouver, ISO, and other styles

23

Li, Chen, Shijie Dai, Aijie Cao, Zhifang Zhou, and Zhimeng Wu. "Design and synthesis of rhamnose-modified exenatide conjugate by sortase A-mediated ligation." Journal of Carbohydrate Chemistry 38, no. 3 (March 24, 2019): 167–78. http://dx.doi.org/10.1080/07328303.2019.1609021.

Full text

APA, Harvard, Vancouver, ISO, and other styles

24

Proft, Thomas. "Sortase-mediated protein ligation: an emerging biotechnology tool for protein modification and immobilisation." Biotechnology Letters 32, no. 1 (September 1, 2009): 1–10. http://dx.doi.org/10.1007/s10529-009-0116-0.

Full text

APA, Harvard, Vancouver, ISO, and other styles

25

Cao, Ting, Jing Lv, Lei Zhang, Guoquan Yan, and Haojie Lu. "Selective Enrichment and Quantification of N-Terminal Glycine Peptides via Sortase A Mediated Ligation." Analytical Chemistry 90, no. 24 (November 30, 2018): 14303–8. http://dx.doi.org/10.1021/acs.analchem.8b03562.

Full text

APA, Harvard, Vancouver, ISO, and other styles

26

Refaei, Mary Anne, Al Combs, Douglas J. Kojetin, John Cavanagh, Carol Caperelli, Mark Rance, Jennifer Sapitro, and Pearl Tsang. "Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy." Journal of Biomolecular NMR 49, no. 1 (December 29, 2010): 3–7. http://dx.doi.org/10.1007/s10858-010-9464-2.

Full text

APA, Harvard, Vancouver, ISO, and other styles

27

Kobashigawa, Yoshihiro, Hiroyuki Kumeta, Kenji Ogura, and Fuyuhiko Inagaki. "Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method." Journal of Biomolecular NMR 43, no. 3 (January 13, 2009): 145–50. http://dx.doi.org/10.1007/s10858-008-9296-5.

Full text

APA, Harvard, Vancouver, ISO, and other styles

28

Boyko, Kristina V., Erin A. Rosenkranz, Derrick M. Smith, Heather L. Miears, Melissa Oueld es cheikh, Micah Z. Lund, Jeffery C. Young, et al. "Sortase-mediated segmental labeling: A method for segmental assignment of intrinsically disordered regions in proteins." PLOS ONE 16, no. 10 (October 28, 2021): e0258531. http://dx.doi.org/10.1371/journal.pone.0258531.

Full text

Abstract:

A significant number of proteins possess sizable intrinsically disordered regions (IDRs). Due to the dynamic nature of IDRs, NMR spectroscopy is often the tool of choice for characterizing these segments. However, the application of NMR to IDRs is often hindered by their instability, spectral overlap and resonance assignment difficulties. Notably, these challenges increase considerably with the size of the IDR. In response to these issues, here we report the use of sortase-mediated ligation (SML) for segmental isotopic labeling of IDR-containing samples. Specifically, we have developed a ligation strategy involving a key segment of the large IDR and adjacent folded headpiece domain comprising the C-terminus of A. thaliana villin 4 (AtVLN4). This procedure significantly reduces the complexity of NMR spectra and enables group identification of signals arising from the labeled IDR fragment, a process we refer to as segmental assignment. The validity of our segmental assignment approach is corroborated by backbone residue-specific assignment of the IDR using a minimal set of standard heteronuclear NMR methods. Using segmental assignment, we further demonstrate that the IDR region adjacent to the headpiece exhibits nonuniform spectral alterations in response to temperature. Subsequent residue-specific characterization revealed two segments within the IDR that responded to temperature in markedly different ways. Overall, this study represents an important step toward the selective labeling and probing of target segments within much larger IDR contexts. Additionally, the approach described offers significant savings in NMR recording time, a valuable advantage for the study of unstable IDRs, their binding interfaces, and functional mechanisms.

APA, Harvard, Vancouver, ISO, and other styles

29

Teschke, Till, Bernhard Geltinger, Alexander Dose, Christian Freund, and Dirk Schwarzer. "Probing the Recognition of Post-Translational Modifications by Combining Sortase-Mediated Ligation and Phage-Assisted Selection." ACS Chemical Biology 8, no. 8 (June 12, 2013): 1692–97. http://dx.doi.org/10.1021/cb4001487.

Full text

APA, Harvard, Vancouver, ISO, and other styles

30

Lee, Taek, Junhong Min, Hidehiko Hirakawa, Teruyuki Nagamune, and Jeong-Woo Choi. "Fusion protein bilayer fabrication composed of recombinant azurin/cytochrome P450 by the sortase-mediated ligation method." Colloids and Surfaces B: Biointerfaces 120 (August 2014): 215–21. http://dx.doi.org/10.1016/j.colsurfb.2014.03.034.

Full text

APA, Harvard, Vancouver, ISO, and other styles

31

Liu, Chenjiang, Yoshihiro Kobashigawa, Soichiro Yamauchi, Natsuki Fukuda, Takashi Sato, Takeshi Masuda, Sumio Ohtsuki, and Hiroshi Morioka. "Convenient method of producing cyclic single-chain Fv antibodies by split-intein-mediated protein ligation and chaperone co-expression." Journal of Biochemistry 168, no. 3 (April 10, 2020): 257–63. http://dx.doi.org/10.1093/jb/mvaa042.

Full text

Abstract:

Abstract Single-chain Fv (scFv) is a recombinant antibody in which the variable regions of the heavy chain (VH) and light chain (VL) are connected by a short flexible polypeptide linker. Compared with monoclonal antibodies, scFvs have the advantages of low-cost production using Escherichia coli and easy genetic manipulation. ScFvs are, therefore, regarded as useful modules for producing next-generation medical antibodies. The practical use of scFvs has been limited due to their aggregation propensity mediated by interchain VH–VL interactions. To overcome this problem, we recently reported a cyclic scFv whose N-terminus and C-terminus were connected by sortase A-mediated ligation. Preparation of cyclic scFv is, however, a time-consuming process. To accelerate the application study of cyclic scFv, we developed a method to produce cyclic scFv by the combined use of a protein ligation technique based on protein trans-splicing reaction (PTS) by split intein and a chaperone co-expression system. This method allows for the preparation of active cyclic scFv from the cytoplasm of E. coli. The present method was applied to the production of cyclic 73MuL9-scFv, a GA-pyridine antibody, as a kind of advanced glycation end-product. These findings are expected to evoke further application study of cyclic scFv.

APA, Harvard, Vancouver, ISO, and other styles

32

Ott, Wolfgang, Thomas Nicolaus, Hermann E. Gaub, and Michael A. Nash. "Sequence-Independent Cloning and Post-Translational Modification of Repetitive Protein Polymers through Sortase and Sfp-Mediated Enzymatic Ligation." Biomacromolecules 17, no. 4 (March 22, 2016): 1330–38. http://dx.doi.org/10.1021/acs.biomac.5b01726.

Full text

APA, Harvard, Vancouver, ISO, and other styles

33

Wu, Zhimeng, Xiaozhong Cheng, Haofei Hong, Xinrui Zhao, and Zhifang Zhou. "New potent and selective αvβ3 integrin ligands: Macrocyclic peptides containing RGD motif synthesized by sortase A-mediated ligation." Bioorganic & Medicinal Chemistry Letters 27, no. 9 (May 2017): 1911–13. http://dx.doi.org/10.1016/j.bmcl.2017.03.035.

Full text

APA, Harvard, Vancouver, ISO, and other styles

34

Wu, Zhi-Meng, Shao-Zhong Liu, Xiao-Zhong Cheng, Xin-Rui Zhao, and Hao-Fei Hong. "High yield synthesis of cyclic analogues of antibacterial peptides P-113 by Sortase A-mediated ligation and their conformation studies." Chinese Chemical Letters 28, no. 3 (March 2017): 553–57. http://dx.doi.org/10.1016/j.cclet.2016.11.001.

Full text

APA, Harvard, Vancouver, ISO, and other styles

35

Krzyscik, Mateusz Adam, Łukasz Opaliński, and Jacek Otlewski. "Novel Method for Preparation of Site-Specific, Stoichiometric-Controlled Dual Warhead Conjugate of FGF2 via Dimerization Employing Sortase A-Mediated Ligation." Molecular Pharmaceutics 16, no. 8 (June 17, 2019): 3588–99. http://dx.doi.org/10.1021/acs.molpharmaceut.9b00434.

Full text

APA, Harvard, Vancouver, ISO, and other styles

36

Madej, Mariusz P., Gregory Coia, Charlotte C. Williams, Joanne M. Caine, Lesley A. Pearce, Rebecca Attwood, Nick A. Bartone, et al. "Engineering of an anti-epidermal growth factor receptor antibody to single chain format and labeling by sortase A-mediated protein ligation." Biotechnology and Bioengineering 109, no. 6 (December 26, 2011): 1461–70. http://dx.doi.org/10.1002/bit.24407.

Full text

APA, Harvard, Vancouver, ISO, and other styles

37

Patterson, Dustin, Benjamin Schwarz, John Avera, Brian Western, Matthew Hicks, Paul Krugler, Matthew Terra, Masaki Uchida, Kimberly McCoy, and Trevor Douglas. "Sortase-Mediated Ligation as a Modular Approach for the Covalent Attachment of Proteins to the Exterior of the Bacteriophage P22 Virus-like Particle." Bioconjugate Chemistry 28, no. 8 (June 30, 2017): 2114–24. http://dx.doi.org/10.1021/acs.bioconjchem.7b00296.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Yamauchi, Soichiro, Yoshihiro Kobashigawa, Natsuki Fukuda, Manaka Teramoto, Yuya Toyota, Chenjiang Liu, Yuka Ikeguchi, et al. "Cyclization of Single-Chain Fv Antibodies Markedly Suppressed Their Characteristic Aggregation Mediated by Inter-Chain VH-VL Interactions." Molecules 24, no. 14 (July 18, 2019): 2620. http://dx.doi.org/10.3390/molecules24142620.

Full text

Abstract:

Single-chain Fv (scFv) antibodies are recombinant proteins in which the variable regions of the heavy chain (VH) and light chain (VL) are connected by a short flexible polypeptide linker. ScFvs have the advantages of easy genetic manipulation and low-cost production using Escherichia coli compared with monoclonal antibodies, and are thus expected to be utilized as next-generation medical antibodies. However, the practical use of scFvs has been limited due to low homogeneity caused by their aggregation propensity mediated by inter-chain VH-VL interactions. Because the interactions between the VH and VL domains of antibodies are generally weak, individual scFvs are assumed to be in equilibrium between a closed state and an open state, in which the VH and VL domains are assembled and disassembled, respectively. This dynamic feature of scFvs triggers the formation of dimer, trimer, and larger aggregates caused by the inter-chain VH-VL interactions. To overcome this problem, the N-terminus and C-terminus were herein connected by sortase A-mediated ligation to produce a cyclic scFv. Open-closed dynamics and aggregation were markedly suppressed in the cyclic scFv, as judged from dynamic light scattering and high-speed atomic force microscopy analyses. Surface plasmon resonance and differential scanning fluorometry analysis revealed that neither the affinity for antigen nor the thermal stability was disrupted by the scFv cyclization. Generality was confirmed by applying the present method to several scFv proteins. Based on these results, cyclic scFvs are expected to be widely utilized in industrial and therapeutic applications.

APA, Harvard, Vancouver, ISO, and other styles

39

Le, Rosemary K., Maryam Raeeszadeh-Sarmazdeh, Eric T. Boder, and Paul D. Frymier. "Sortase-Mediated Ligation of PsaE-Modified Photosystem I from Synechocystis sp. PCC 6803 to a Conductive Surface for Enhanced Photocurrent Production on a Gold Electrode." Langmuir 31, no. 3 (January 8, 2015): 1180–88. http://dx.doi.org/10.1021/la5031284.

Full text

APA, Harvard, Vancouver, ISO, and other styles

40

Wu, Si, and Thomas Proft. "The use of sortase-mediated ligation for the immobilisation of bacterial adhesins onto fluorescence-labelled microspheres: a novel approach to analyse bacterial adhesion to host cells." Biotechnology Letters 32, no. 11 (July 11, 2010): 1713–18. http://dx.doi.org/10.1007/s10529-010-0349-y.

Full text

APA, Harvard, Vancouver, ISO, and other styles

41

Nikghalb, Keyvan D., Nicholas M. Horvath, Jesse L. Prelesnik, Orion G. B. Banks, Pavel A. Filipov, R. David Row, Travis J. Roark, and John M. Antos. "Expanding the Scope of Sortase-Mediated Ligations by Using Sortase Homologues." ChemBioChem 19, no. 2 (December 18, 2017): 185–95. http://dx.doi.org/10.1002/cbic.201700517.

Full text

APA, Harvard, Vancouver, ISO, and other styles

42

Schmohl, Lena, and Dirk Schwarzer. "Sortase-mediated ligations for the site-specific modification of proteins." Current Opinion in Chemical Biology 22 (October 2014): 122–28. http://dx.doi.org/10.1016/j.cbpa.2014.09.020.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

David Row, R., Travis J. Roark, Marina C. Philip, Lorena L. Perkins, and John M. Antos. "Enhancing the efficiency of sortase–mediated ligations through nickel–peptide complex formation." Chemical Communications 51, no. 63 (2015): 12548–51. http://dx.doi.org/10.1039/c5cc04657b.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Zuo, Chong, Ruichao Ding, Xiangwei Wu, Yuanxia Wang, Guo-Chao Chu, Lu-Jun Liang, Huasong Ai, et al. "Thioester‐Assisted Sortase‐A ‐ Mediated Ligation." Angewandte Chemie International Edition, May 6, 2022. http://dx.doi.org/10.1002/anie.202201887.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Zuo, Chong, Ruichao Ding, Xiangwei Wu, Yuanxia Wang, Guo-Chao Chu, Lu-Jun Liang, Huasong Ai, et al. "Thioester‐Assisted Sortase‐A ‐ Mediated Ligation." Angewandte Chemie, May 6, 2022. http://dx.doi.org/10.1002/ange.202201887.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Dolan, Jonathan P., Darren C. Machin, Simone Dedola, Robert A. Field, Michael E. Webb, and W. Bruce Turnbull. "Synthesis of cholera toxin B subunit glycoconjugates using site-specific orthogonal oxime and sortase ligation reactions." Frontiers in Chemistry 10 (September 14, 2022). http://dx.doi.org/10.3389/fchem.2022.958272.

Full text

Abstract:

The chemoenzymatic synthesis of a series of dual N- and C-terminal–functionalized cholera toxin B subunit (CTB) glycoconjugates is described. Mucin 1 peptides bearing different levels of Tn antigen glycosylation [MUC1(Tn)] were prepared via solid-phase peptide synthesis. Using sortase-mediated ligation, the MUC1(Tn) epitopes were conjugated to the C-terminus of CTB in a well-defined manner allowing for high-density display of the MUC1(Tn) epitopes. This work explores the challenges of using sortase-mediated ligation in combination with glycopeptides and the practical considerations to obtain high levels of conjugation. Furthermore, we describe methods to combine two orthogonal labeling methodologies, oxime- and sortase-mediated ligation, to expand the biochemical toolkit and produce dual N- and C-terminal–labeled conjugates.

APA, Harvard, Vancouver, ISO, and other styles

47

Bierlmeier, Jan, Miguel Álvaro‐Benito, Maren Scheffler, Kristina Sturm, Luisa Rehkopf, Christian Freund, and Dirk Schwarzer. "Sortase‐Mediated Multi‐Fragment Assemblies by Ligation Site Switching." Angewandte Chemie International Edition 61, no. 5 (December 13, 2021). http://dx.doi.org/10.1002/anie.202109032.

Full text

APA, Harvard, Vancouver, ISO, and other styles

48

Tsukiji, Shinya, and Teruyuki Nagamune. "ChemInform Abstract: Sortase-Mediated Ligation: A Gift from Gram-Positive Bacteria to Protein Engineering." ChemInform 40, no. 20 (May 19, 2009). http://dx.doi.org/10.1002/chin.200920264.

Full text

APA, Harvard, Vancouver, ISO, and other styles

49

Apostolos, Alexis J., Joey J. Kelly, George M. Ongwae, and Marcos Moura Pires. "Structure Activity Relationship of the Stem Peptide in Sortase A mediated Ligation from Staphylococcus aureus." ChemBioChem, August 26, 2022. http://dx.doi.org/10.1002/cbic.202200412.

Full text

APA, Harvard, Vancouver, ISO, and other styles

50

Krzyscik, Mateusz Adam, Aleksandra Sokolowska-Wedzina, Karolina Jendryczko, Marta Pozniak, Daria Nawrocka, Natalia Porebska, Malgorzata Zakrzewska, Jacek Otlewski, Anna Szlachcic, and Lukasz Opalinski. "Preparation of Site-Specific Cytotoxic Protein Conjugates via Maleimide-thiol Chemistry and Sortase A-Mediated Ligation." Journal of Visualized Experiments, no. 167 (January 5, 2021). http://dx.doi.org/10.3791/61918.

Full text

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!