ISSN Print 2500–1094
ISSN Online 2542–1204
BIOMEDICAL JOURNAL OF PIROGOV UNIVERSITY (MOSCOW, RUSSIA)
Copyright: © 2025 by the authors. Licensee: Pirogov University.
This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (CC BY).
This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (CC BY).
ORIGINAL RESEARCH
Comparative imaging of the HAEE-CY5 and ЕЕАН-СУ5 tetrapeptide binding to the Aβ aggregates on the SH-SY5Y cells
About authors
1 Research Institute of Translational Medicine, Pirogov Russian National Research Medical University, Moscow, Russia
2 Institute of Biomedical Engineering, MISIS University of Science and Technology, Moscow, Russia
Correspondence should be addressed: Anna V. Ivanova
Ostrovityanova, 1, str.1, Moscow, 117513, Russia; ur.xednay@tirofsof.repus
About paper
Funding: the work was carried out under the State Assignment "Development of a radiopharmaceutical for the diagnosis of Alzheimer's disease using the HAEE tetrapeptide as a vector molecule", EGISU R&D registration number 1024110600012-8-3.2.25;3.2.26;3.2.12.
Author contribution: Ivanova AV — literature review, manuscript writing; Chmelyuk NS — fixation, cell sample preparation for microscopic imaging, image acquisition and analysis using a confocal microscope; Kuzmichev IA — synthesis of Ac-HAEEGGGGK(ε-Cy5)-NH2 and Ac-EEAHGGGGK(ε-Cy5)-NH2 fluorescent peptides; Shilyaeva MI — cell sample preparation; Abakumov MA — goal setting, developing the study design, manuscript writing; all the authors contributed to preparation of the paper equally, they confirmed compliance of their authorship with the international ICMJE criteria.
Received: 2025-10-15
Accepted: 2025-11-13
Published online: 2025-11-24
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Due to high diagnostic value of β-amyloid aggregates, the target ligands capable of specific binding to abnormal Aβ aggregates are of special interest. The study aimed to perform comparative characterization of the HAEE-Сy5 (Ac-His-Ala-Glu-Glu-Gly-Gly-Gly-Gly-Lys(ε-Cy5)-NH2) and EEAH-Cy5 (Ac-Glu-Glu-Ala-His-GlyGly-Gly-Gly-Lys(ε-Cy5)-NH2) tetrapeptide capability of binding to the Aβ aggregates in the SH-SY5Y human neuroblastoma cell line by confocal microscopy. It has been shown that the HAEE-Cy5 tetrapeptide demonstrates specific binding yielding typical cytoplasmic clusters and clear co-localization with the amyloid aggregates, while the EEAH-Cy5 peptide with the inverted sequence totally loses the binding capability. Quantification has confirmed high specificity of the HAEECy5 binding to the Aβ aggregates (Manders' colocalization coefficient 0.58 ± 0.03). It has been found that the histidine N-terminal position is a critical determinant of the interaction specificity. The findings offer the prospects of using the HAEE peptide as a platform for the development of targeted disgnostic systems for amyloid disorder imaging.
Keywords: HAEE peptide, EEAH peptide, Aβ aggregates, SH-SY5Y, Alzheimer's disease