prikaz prve stranice dokumenta Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein
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Scientific paper - Original scientific paper
Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein
PLoS ONE, 13 (2018), e0191162; 18. https://doi.org/10.1371/journal.pone.0191162
Yerabham, Antony S. K.; Müller-Schiffmann, Andreas; Ziehm, Tamar; Stadler, Andreas; Köber, Sabrina; Indurkhya, Xela; Marreiros, Rita; Trossbach, Svenja V.; Bradshaw, Nicholas J.; Prikulis, Ingrid; Willbold, Dieter; Weiergräber, Oliver H.; Korth, Carsten

Institutional repository: Repository of the University of Rijeka, Faculty of Biotechnology and Drug Development

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Yerabham, A. S. K., Müller Schiffmann, A., Ziehm, T., Stadler, A., Köber, S., Indurkhya, X. ... Korth, C. (2018). Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein. PLoS ONE, 13. (e0191162). doi: 10.1371/journal.pone.0191162

Yerabham, Antony S. K., et al. "Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein." PLoS ONE, vol. 13, no. e0191162, 2018. https://doi.org/10.1371/journal.pone.0191162

Yerabham, Antony S. K., Andreas Müller Schiffmann, Tamar Ziehm, Andreas Stadler, Sabrina Köber, Xela Indurkhya, Rita Marreiros, et al. "Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein." PLoS ONE 13, no. e0191162 (2018). https://doi.org/10.1371/journal.pone.0191162

Yerabham, A. S. K., et al. (2018) 'Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein', PLoS ONE, 13(e0191162). doi: 10.1371/journal.pone.0191162

Yerabham ASK, Müller Schiffmann A, Ziehm T, Stadler A, Köber S, Indurkhya X, and sur.. Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein. PLoS ONE [Internet]. 2018 January 11 [cited 2024 November 17];13(e0191162). doi: 10.1371/journal.pone.0191162

A. S. K. Yerabham, et al., "Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein", PLoS ONE, vol. 13, no. e0191162, January 2018. [Online]. Available at: https://urn.nsk.hr/urn:nbn:hr:193:359049. [Accessed: 17 November 2024]

Metadata
Title (english)Biophysical insights from a single chain camelid antibody directed against the Disrupted-in-Schizophrenia 1 protein
AuthorAntony S. K. Yerabham
AuthorAndreas Müller-Schiffmann
AuthorTamar Ziehm
AuthorAndreas Stadler
AuthorSabrina Köber
AuthorXela Indurkhya
AuthorRita Marreiros
AuthorSvenja V. Trossbach
AuthorNicholas J. Bradshaw
AuthorIngrid Prikulis
AuthorDieter Willbold
AuthorOliver H. Weiergräber
AuthorCarsten Korth
Author's institutionUniversity of Rijeka
(Faculty of Biotechnology and Drug Development)
Scientific / art field,
discipline and subdiscipline		BIOTECHNICAL SCIENCES
Biotechnology
Biology
Abstract (english)
Accumulating evidence suggests an important role for the Disrupted-in-Schizophrenia 1 (DISC1) protein in neurodevelopment and chronic mental illness. In particular, the C-terminal 300 amino acids of DISC1 have been found to mediate important protein-protein interactions and to harbor functionally important phosphorylation sites and disease-associated polymorphisms. However, long disordered regions and oligomer-forming subdomains have so far impeded structural analysis. VHH domains derived from camelid heavy chain only antibodies are minimal antigen binding modules with appreciable solubility and stability, which makes them well suited for the stabilizing proteins prior to structural investigation. Here, we report on the generation of a VHH domain derived from an immunized Lama glama, displaying high affinity for the human DISC1 C region (aa 691±836), and its characterization by surface plasmon resonance, size exclusion chromatography and immunological techniques. The VHH-DISC1 (C region) complex was also used for structural investigation by small angle X-ray scattering analysis. In combination with molecular modeling, these data support predictions regarding the three-dimensional fold of this DISC1 segment as well as its steric arrangement in complex with our VHH antibody.
Languageenglish
Publication typeScientific paper - Original scientific paper
Publication statusPublished
Peer reviewPeer review - international
Publication versionPublished version
Journal titlePLoS ONE
Numberingvol. 13, no. e0191162, 18
e-ISSN1932-6203
DOIhttps://doi.org/10.1371/journal.pone.0191162
URN:NBNurn:nbn:hr:193:359049
Publication2018-01-11
Document URLhttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0191162
Type of resourceText
Access conditionsOpen access
Terms of useLicence Attribution 4.0 International (CC BY 4.0) icon
Created on2018-09-14 11:48:51