This preprint is under consideration at Scientific Reports. A preprint is a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Learn more about In Review
Research Article
Kristina N. Woods
Ludwig Maximilian University of Munich
Corresponding Author
License:
This work is licensed under a CC BY 4.0 License. Read Full License
In this investigation, we report the effect on the microscopic dynamics and interactions of the cytokine interferon gamma (IFN-g) and antibodies to IFN-g (anti-IFN-g) and to the interferon gamma receptor 1 (anti-IFNGR1) prepared in exceptionally dilute solutions of initial proteins. Using both THz spectroscopy and molecular dynamics (MD) simulations we have uncovered that the high dilution method of sample preparation results in the reorganization of the sample surface residue dynamics at the solvent-protein interface that leads to both structural and kinetic heterogeneous dynamics that ultimately create interactions that enhance the binding probability of the antigen binding site. Our results indicate that the modified interfacial dynamics of anti-IFN-g and anti-IFGNR1 that we probe experimentally are directly associated with alterations in the complementarity regions of the distinct antibodies that designate both antigen-antibody affinity and recognition.
Keywords
antibodies, highly diluted biologics, microscopic interactions
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
Figure 7
Figure 8
Figure 9
Figure 10
Figure 11
Figure 12
Figure 13
Figure 14
Figure 15
This preprint is available for download as a PDF.
Competing interest reported. The author declares the following potential conflicts of interest with respect to the research, authorship, and/or publication of this article: OOO “NPF “MATERIA MEDICA HOLDING” (Moscow, Russia) sponsored the study. Different technological versions of HD-anti- IFN-g are the substances (single or one among other components) for commercial drugs produced or produced and marked by OOO “NPF “MATERIA MEDICA HOLDING”. All HD-samples tested in the study were prepared and provided by ООО “NPF “MATERIA MEDICA HOLDING”. Several patents on these substances belong to OOO “NPF “MATERIA MEDICA HOLDING”. The author has disclosed those interests fully to Scientific Reports.
This is a list of supplementary files associated with this preprint. Click to download.
Loading...
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Under Review
Version 1
Posted 16 Mar, 2021
No community comments so far
Reviewer #1 agreed
On 24 Mar, 2021
Reviewer #3 agreed
On 24 Mar, 2021
Reviewer #7 agreed
On 24 Mar, 2021
Reviewer #8 agreed
On 24 Mar, 2021
Reviewer #5 agreed
On 24 Mar, 2021
Reviewer #6 agreed
On 24 Mar, 2021
Reviewers invited
Invitations sent on 15 Mar, 2021
Editor assigned
On 15 Mar, 2021
Editor invited
On 15 Mar, 2021
Submission checks complete
On 15 Mar, 2021
First submitted
On 01 Mar, 2021
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
Learn more about our company.
This preprint is under consideration at Scientific Reports. A preprint is a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Learn more about In Review
Research Article
Kristina N. Woods
Ludwig Maximilian University of Munich
Corresponding Author
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Under Review
Version 1
Posted 16 Mar, 2021
No community comments so far
Reviewer #1 agreed
On 24 Mar, 2021
Reviewer #3 agreed
On 24 Mar, 2021
Reviewer #7 agreed
On 24 Mar, 2021
Reviewer #8 agreed
On 24 Mar, 2021
Reviewer #5 agreed
On 24 Mar, 2021
Reviewer #6 agreed
On 24 Mar, 2021
Reviewers invited
Invitations sent on 15 Mar, 2021
Editor assigned
On 15 Mar, 2021
Editor invited
On 15 Mar, 2021
Submission checks complete
On 15 Mar, 2021
First submitted
On 01 Mar, 2021
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
License:
This work is licensed under a CC BY 4.0 License. Read Full License
In this investigation, we report the effect on the microscopic dynamics and interactions of the cytokine interferon gamma (IFN-g) and antibodies to IFN-g (anti-IFN-g) and to the interferon gamma receptor 1 (anti-IFNGR1) prepared in exceptionally dilute solutions of initial proteins. Using both THz spectroscopy and molecular dynamics (MD) simulations we have uncovered that the high dilution method of sample preparation results in the reorganization of the sample surface residue dynamics at the solvent-protein interface that leads to both structural and kinetic heterogeneous dynamics that ultimately create interactions that enhance the binding probability of the antigen binding site. Our results indicate that the modified interfacial dynamics of anti-IFN-g and anti-IFGNR1 that we probe experimentally are directly associated with alterations in the complementarity regions of the distinct antibodies that designate both antigen-antibody affinity and recognition.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
Figure 7
Figure 8
Figure 9
Figure 10
Figure 11
Figure 12
Figure 13
Figure 14
Figure 15
This preprint is available for download as a PDF.
Loading...