Correction
Affiliation:
1Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, 119334 Moscow, Russia
Email: maria.g.gorobets@gmail.com
ORCID: https://orcid.org/0000-0002-2946-0495
,
Affiliation:
1Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, 119334 Moscow, Russia
ORCID: https://orcid.org/0009-0002-9674-5586
,
Affiliation:
1Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, 119334 Moscow, Russia
ORCID: https://orcid.org/0000-0002-8876-574X
,
Affiliation:
1Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, 119334 Moscow, Russia
2N.N. Blokhin National Medical Research Center of Oncology, 115478 Moscow, Russia
3Laboratory of Experimental Oncology, Research Institute of Molecular and Cellular Medicine, RUDN University, 117198 Moscow, Russia
ORCID: https://orcid.org/0000-0003-4006-9320
,
Affiliation:
1Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, 119334 Moscow, Russia
ORCID: https://orcid.org/0000-0002-5490-5652
,
Affiliation:
1Emanuel Institute of Biochemical Physics of Russian Academy of Sciences, 119334 Moscow, Russia
ORCID: https://orcid.org/0000-0001-6367-0923
Explor Drug Sci. 2025;3:1008130 DOl: https://doi.org/10.37349/eds.2025.1008130
Received: Accepted: Published: September 24, 2025
Correction to “
In the recently published article, an error was identified in the description of the molecular interactions (in the section “Conjugation of FA residue to serum albumin”). The article incorrectly stated that “For a mixture of bovine albumin and NHS-ester of FA, it was shown an engagement in interaction via different mechanisms of the following listed in the brackets amino acid residues: hydrogen bonding (Tyr149, Tyr340, Glu152, Glu339, Gln220, His289, Val342), π-π interaction (Tyr156), hydrophobic interaction (Lys187, Arg194, Arg256).” The correct statement is that “For a mixture of bovine albumin and NHS-ester of FA, it was shown an engagement in interaction via different mechanisms of the following listed in the brackets amino acid residues: hydrogen bonding (Tyr149, Tyr340, Glu152, Glu339, Gln220, His289, Val342), π-π and/or hydrophobic interactions (Tyr156, Lys187, Arg194, Arg256).” This has now been amended in the HTML and PDF versions of the article.
The original uncorrected PDF can be accessed from https://www.explorationpub.com/uploads/er1008101.pdf
Copyright: © The Author(s) 2025. This is an Open Access article licensed under a Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, sharing, adaptation, distribution and reproduction in any medium or format, for any purpose, even commercially, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
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