Evidence map›Paper›PMID 40085160›Full record

ArticleMolecular biology reports2025

Deciphering aptamer-protein interactions for bovine sperm sorting through in silico and in vitro studies.

Sumit Kumar Singh, Manya Mathur, Himanshu Kamboj, Jai Kumar Kaushik, Ashok Kumar Mohanty, Sudarshan Kumar

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Article in Molecular biology reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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Authors and funding

6 authors.

Sumit Kumar SinghNational Dairy Research Institute (ICAR), Karnal, India.
Manya MathurNational Dairy Research Institute (ICAR), Karnal, India.
Himanshu KambojAmity Institute of Biotechnology, Amity University, Noida, India.
Jai Kumar KaushikNational Dairy Research Institute (ICAR), Karnal, India.
Ashok Kumar MohantyNational Dairy Research Institute (ICAR), Karnal, India.
Sudarshan KumarNational Dairy Research Institute (ICAR), Karnal, India. kumarsudershan@gmail.com.

Funding

Indian Council of Agricultural Research 1006660
6 · The paper itself

Abstract

backgroundIn recent years, aptamers have emerged as versatile molecular tools with promising applications in various fields, including diagnostics and therapeutics. In livestock reproduction, their application holds promise for improving the sorting and identification of X and Y chromosome-bearing sperm cells, which is essential for increasing productivity in the dairy and beef industries.

methodThis study utilized seven rounds of Cell-SELEX using bovine X and Y sperm cells to isolate specific aptamers that target these cells. A comprehensive in-silico analysis was conducted to evaluate the binding interactions between the selected aptamer sequences and the differentially expressed plasma membrane proteins of X and Y sperm cells.

resultThe analysis identified the aptamer sequences APT1X, APT2X, and APT5X as having the most stable interactions with the X sperm surface proteins TLR8 (Toll-like receptor 8), CLRN3, and TLR7 (Toll-like receptor 7), respectively. APT2Y exhibited a relatively high affinity for the protein SCAMP1, a Y-sperm-specific protein. Aptamer‒protein interactions are characterized by hydrogen bonds and hydrophobic contacts. Notably, APT1X formed the greatest number of hydrogen bonds with the polar residues of TLR8, whereas TLR7-APT5X interactions exhibited the greatest number of hydrophobic contacts.

conclusionThe use of in-silico analysis for evaluating the interaction between candidate aptamer sequences and differentially expressed X and Y bovine sperm proteins provides valuable insights. This approach might facilitate the sorting of bovine X and Y sperm cells, contributing to advancements in livestock reproduction strategies.

Indexed as

Aptamers, NucleotideSpermatozoaAnimalsCattleCell SeparationComputer SimulationMaleMembrane ProteinsProtein BindingSELEX Aptamer TechniqueX ChromosomeY ChromosomeAptamers, NucleotideMembrane ProteinsAptamersBovineCell-SELEXIn silico analysisInteraction analysisSemen sexing

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.