A novel thrombin inhibitory peptide discovered from leech using affinity chromatography combined with ultra-high performance liquid chromatography-high resolution mass spectroscopy
Research article published in J Chromatogr B Analyt Technol Biomed Life Sci (2020)
Abstract
Thrombin (THR) inhibitors play an important role in the treatment of thrombotic diseases. This study established a THR-based bio-specific extraction coupled with affinity chromatography and ultra-high performance liquid chromatography-high resolution mass spectroscopy (UPLC-HR-MS) analysis method to screen and identify THR ligands in Leech. After evaluating the reliability of the screening method using positive control drug (hirudin), it was successfully used to screen the potential active constituents in leech. And a comprehensive analysis of the peptides in leech elution was performed by UPLC-HR-MS, a total of 34 peptides were identified. At the same time, anti-THR activity was explored and inferred by searching databases and published literature. As a result, six peptides were discovered to be potential active compounds in leech. Further, the six peptides were synthesized and in vitro enzymatic activity assay was performed. Finally, SYELPDGQVITIGNER was screened as an anti-THR peptide with an IC50 value of 255.75 µM and it was discovered for the first time from Whitmania pigra Whitman and Hirudo nipponica Whitman. The molecular docking study showed that THR inhibitory activity of the polypeptide was mainly attributed to the hydrogen bond interactions, van der Waals forces and electrostatic interactions interaction between polypeptide and THR. These results suggest that the polypeptide is a potential natural THR inhibitor that can be used as anticoagulant.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Resumen
Thrombin (THR) inhibitors play an important role in the treatment of thrombotic diseases. This study established a THR-based bio-specific extraction coupled with affinity chromatography and ultra-high performance liquid chromatography-high resolution mass spectroscopy (UPLC-HR-MS) analysis method to screen and...
Por qué esto importa para la hirudoterapia
Este estudio estableció un método de extracción bioespecífica basado en trombina, utilizando cromatografía de afinidad y UPLC-HR-MS para cribar e identificar ligandos de trombina en material de sanguijuela, validando el abordaje con hirudina como control positivo. De 34 péptidos identificados, se seleccionaron seis para su síntesis y ensayo enzimático in vitro, obteniéndose un péptido de 16 aminoácidos (SYELPDGQVITIGNER) con actividad inhibitoria de la trombina (IC50 de 255,75 µM), descubierto por primera vez a partir de Whitmania pigra e Hirudo nipponica. Este trabajo es directamente relevante para el ámbito de la ASH, ya que identifica un nuevo péptido anticoagulante potencial procedente de sanguijuelas. La salvedad es que estos hallazgos se basan únicamente en un ensayo enzimático in vitro y en acoplamiento molecular; no se presentan datos in vivo, clínicos ni de hirudoterapia en organismos completos, y la relevancia terapéutica está por establecer.
Citación
A novel thrombin inhibitory peptide discovered from leech using affinity chromatography combined with ultra-high performance liquid chromatography-high resolution mass spectroscopy.
Huang Q et al. · J Chromatogr B Analyt Technol Biomed Life Sci, 2020
Contexto clínico relacionado
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Añadido a la biblioteca ASH: May 27, 2026 · Última actualización del sitio: 18 de junio de 2026