Recombinant decorsin: dynamics of the RGD recognition site
Research article published in Protein science : a publication of the Protein Society (2000)
Abstract
Decorsin is an antagonist of integrin alphaIIbbeta3 and a potent platelet aggregation inhibitor. A synthetic gene encoding decorsin, originally isolated from the leech Macrobdella decora, was designed, constructed, and expressed in Escherichia coli. The synthetic gene was fused to the stII signal sequence and expressed under the transcriptional control of the E. coli alkaline phosphatase promoter. The protein was purified by size-exclusion filtration of the periplasmic contents followed by reversed-phase high-performance liquid chromatography. Purified recombinant decorsin was found to be indistinguishable from leech-derived decorsin based on amino acid composition, mass spectral analysis, and biological activity assays. Complete sequential assignments of 1H and proton bound 13C resonances were established. Stereospecific assignments of 21 of 25 nondegenerate b-methylene groups were determined. The RGD adhesion site recognized by integrin receptors was found at the apex of a most exposed hairpin loop. The dynamic behavior of decorsin was analyzed using several independent NMR parameters. Although the loop containing the RGD sequence is the most flexible one in decorsin, the conformation of the RGD site itself is more restricted than in other proteins with similar activities.
Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.
Resumen
Decorsin is an antagonist of integrin alphaIIbbeta3 and a potent platelet aggregation inhibitor.
Por qué esto importa para la hirudoterapia
This study describes the recombinant expression, purification, and NMR-based structural characterization of decorsin, a potent integrin αIIbβ3 antagonist and platelet aggregation inhibitor originally isolated from the leech Macrobdella decora. A synthetic gene was expressed in E. coli, and the recombinant protein was confirmed indistinguishable from leech-derived decorsin by composition, mass, and bioactivity. The RGD recognition site was localized to the apex of an exposed, flexible hairpin loop, though the RGD conformation itself was more restricted than in comparable proteins. This work is directly relevant to ASH's domain as it advances structural understanding of a leech-secreted antithrombotic protein and validates recombinant production. The study is purely biophysical/biochemical with no in vivo or clinical data.
Citación
Recombinant decorsin: dynamics of the RGD recognition site
Krezel AM et al. · Protein science : a publication of the Protein Society, 2000
Contexto clínico relacionado
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Añadido a la biblioteca ASH: May 27, 2026 · Última actualización del sitio: June 18, 2026