Peer-reviewedCC BY-NC-NDACS omega
DSC Study of Conjugated Recombinant Antigen Solution
- 1National Research Lobachevsky State University of Nizhny Novgorod , ,
- 2RPC “Diagnostic Systems” Ltd. , ,
Abstract
In this study, we carried out series of measurements to determine the thermal characteristics of horseradish peroxidase conjugate of recombinant antigen human immunodeficiency virus type 1 group M gp41 solutions using differential scanning calorimetry methods. For the first time, the conditions for the DSC experiment were selected for the systems in question including temperature range, scanning speed, sample masses. In the temperature range (−80) to 30 °C, crystallization of excess water was observed. Then, fusion of water ice occurred. In the work, qualitative patterns were obtained in the change in thermal properties of the AHIV-p-1030 solutions depending on the antigen concentration.
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BibTeX
@article{markin2026study,
title = {{DSC Study of Conjugated Recombinant Antigen Solution}},
author = {Alexey V. Markin and Semen S. Sologubov and Vladislav S. Lysyy and Roman O. Chirkov and Nadezhda M. Denisova},
journal = {ACS omega},
year = {2026},
month = oct,
doi = {10.1021/acsomega.6c05500},
url = {https://europepmc.org/article/PMC/PMC13670311},
note = {CC BY-NC-ND},
}
RIS
TY - JOUR
TI - DSC Study of Conjugated Recombinant Antigen Solution
AU - Alexey V. Markin
AU - Semen S. Sologubov
AU - Vladislav S. Lysyy
AU - Roman O. Chirkov
AU - Nadezhda M. Denisova
PY - 2026
DA - 2026/10/02
JO - ACS omega
DO - 10.1021/acsomega.6c05500
UR - https://europepmc.org/article/PMC/PMC13670311
AB - In this study, we carried out series of measurements to determine the thermal characteristics of horseradish peroxidase conjugate of recombinant antigen human immunodeficiency virus type 1 group M gp41 solutions using differential scanning calorimetry methods. For the first time, the conditions for the DSC experiment were selected for the systems in question including temperature range, scanning speed, sample masses. In the temperature range (−80) to 30 °C, crystallization of excess water was observed. Then, fusion of water ice occurred. In the work, qualitative patterns were obtained in the change in thermal properties of the AHIV-p-1030 solutions depending on the antigen concentration.
SN - 2470-1343
ER -