View in EDS HTML Full Text PDF Full Text

Enhancing the Thermostability and solubility of a single-domain catalytic antibody.

Saved in:
Bibliographic Details
Title: Enhancing the Thermostability and solubility of a single-domain catalytic antibody.
Authors: Cui, Yunhang1 (AUTHOR), Zhou, Xuchen2 (AUTHOR), Li, Sainan2 (AUTHOR), Chen, Jingfei3 (AUTHOR), Qin, Mingming3 (AUTHOR), An, Liaoyuan3 (AUTHOR), Wang, Yefei3 (AUTHOR), Yao, Lishan3 (AUTHOR)
Source: PEDS: Protein Engineering, Design & Selection. 2025, Vol. 38, p1-8. 8p.
Subjects: Protein stability, Protein engineering, Monoclonal antibodies, Helicobacter pylori, Disulfides, Thermal stability, Molecular dynamics
Abstract: Catalytic antibodies have the ability to bind to and degrade antigens, offering a significant potential for therapeutic use. The light chain of an antibody, UA15-L, can cleave the peptide bond of Helicobacter pylori urease, thus inhibiting the spread of the bacteria. However, the variable domain of UA15-L has a poor thermostability and solubility. In this study, we employed a combined computational and experimental approach to enhance the protein's stability and solubility properties. The protein unfolding hotspots were initially identified using molecular dynamics simulations. Following this, a disulfide bond was designed in an unfolding hotspot to stabilize the protein. Subsequently, protein solubility was enhanced with the assistance of computational methods by introducing polar or charged residues on the protein surface. The combination of multiple mutations resulted in UA15-L variable domain variants with improved thermostability, solubility, expression, and enhanced activity at elevated temperatures. These variants represent promising candidates for further engineering of catalytic activity and specificity. [ABSTRACT FROM AUTHOR]
Copyright of PEDS: Protein Engineering, Design & Selection is the property of Oxford University Press / USA and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
Full text is not displayed to guests.
FullText Links:
  – Type: pdflink
Text:
  Availability: 1
Header DbId: egs
DbLabel: Engineering Source
An: 191816611
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Enhancing the Thermostability and solubility of a single-domain catalytic antibody.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Cui%2C+Yunhang%22">Cui, Yunhang</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Zhou%2C+Xuchen%22">Zhou, Xuchen</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Li%2C+Sainan%22">Li, Sainan</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Chen%2C+Jingfei%22">Chen, Jingfei</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Qin%2C+Mingming%22">Qin, Mingming</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22An%2C+Liaoyuan%22">An, Liaoyuan</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Wang%2C+Yefei%22">Wang, Yefei</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Yao%2C+Lishan%22">Yao, Lishan</searchLink><relatesTo>3</relatesTo> (AUTHOR)
– Name: TitleSource
  Label: Source
  Group: Src
  Data: <searchLink fieldCode="JN" term="%22PEDS%3A+Protein+Engineering%2C+Design+%26+Selection%22">PEDS: Protein Engineering, Design & Selection</searchLink>. 2025, Vol. 38, p1-8. 8p.
– Name: Subject
  Label: Subjects
  Group: Su
  Data: <searchLink fieldCode="DE" term="%22Protein+stability%22">Protein stability</searchLink><br /><searchLink fieldCode="DE" term="%22Protein+engineering%22">Protein engineering</searchLink><br /><searchLink fieldCode="DE" term="%22Monoclonal+antibodies%22">Monoclonal antibodies</searchLink><br /><searchLink fieldCode="DE" term="%22Helicobacter+pylori%22">Helicobacter pylori</searchLink><br /><searchLink fieldCode="DE" term="%22Disulfides%22">Disulfides</searchLink><br /><searchLink fieldCode="DE" term="%22Thermal+stability%22">Thermal stability</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+dynamics%22">Molecular dynamics</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Catalytic antibodies have the ability to bind to and degrade antigens, offering a significant potential for therapeutic use. The light chain of an antibody, UA15-L, can cleave the peptide bond of Helicobacter pylori urease, thus inhibiting the spread of the bacteria. However, the variable domain of UA15-L has a poor thermostability and solubility. In this study, we employed a combined computational and experimental approach to enhance the protein's stability and solubility properties. The protein unfolding hotspots were initially identified using molecular dynamics simulations. Following this, a disulfide bond was designed in an unfolding hotspot to stabilize the protein. Subsequently, protein solubility was enhanced with the assistance of computational methods by introducing polar or charged residues on the protein surface. The combination of multiple mutations resulted in UA15-L variable domain variants with improved thermostability, solubility, expression, and enhanced activity at elevated temperatures. These variants represent promising candidates for further engineering of catalytic activity and specificity. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of PEDS: Protein Engineering, Design & Selection is the property of Oxford University Press / USA and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=191816611
RecordInfo BibRecord:
  BibEntity:
    Identifiers:
      – Type: doi
        Value: 10.1093/protein/gzaf002
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 8
        StartPage: 1
    Subjects:
      – SubjectFull: Protein stability
        Type: general
      – SubjectFull: Protein engineering
        Type: general
      – SubjectFull: Monoclonal antibodies
        Type: general
      – SubjectFull: Helicobacter pylori
        Type: general
      – SubjectFull: Disulfides
        Type: general
      – SubjectFull: Thermal stability
        Type: general
      – SubjectFull: Molecular dynamics
        Type: general
    Titles:
      – TitleFull: Enhancing the Thermostability and solubility of a single-domain catalytic antibody.
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Cui, Yunhang
      – PersonEntity:
          Name:
            NameFull: Zhou, Xuchen
      – PersonEntity:
          Name:
            NameFull: Li, Sainan
      – PersonEntity:
          Name:
            NameFull: Chen, Jingfei
      – PersonEntity:
          Name:
            NameFull: Qin, Mingming
      – PersonEntity:
          Name:
            NameFull: An, Liaoyuan
      – PersonEntity:
          Name:
            NameFull: Wang, Yefei
      – PersonEntity:
          Name:
            NameFull: Yao, Lishan
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 01
              Text: 2025
              Type: published
              Y: 2025
          Identifiers:
            – Type: issn-print
              Value: 17410126
          Numbering:
            – Type: volume
              Value: 38
          Titles:
            – TitleFull: PEDS: Protein Engineering, Design & Selection
              Type: main
ResultId 1