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Novel disintegrin-like peptides derived from an amphibian skin cDNA sequence of Hypsiboas punctatus
Journal of Peptide Science ( IF 2.1 ) Pub Date : 2021-12-02 , DOI: 10.1002/psc.3382
Diego A T Pires 1 , Luisa M R A Tacca 2 , Joseph E Aslan 3 , André M Murad 2 , Claudia J Nascimento 4 , Eder A Barbosa 2 , Carlos Bloch 2
Affiliation  

Disintegrins comprise a family of small proteins that bind to and alter the physiological function of integrins, especially integrins that mediate platelet aggregation in blood. Here, we report a lysine-glycine-aspartic acid (KGD) disintegrin-like motif present in a 15-amino acid residue peptide identified in a cDNA library of the amphibian Hypsiboas punctatus skin. The original peptide sequence was used as a template from which five new analogs were designed, chemically synthesized by solid phase, and tested for disintegrin activity and tridimensional structural studies using NMR spectroscopy. The original amphibian peptide had no effect on integrin-mediated responses. Nevertheless, derived peptide analogs inhibited integrin-mediated platelet function, including platelet spreading on fibrinogen.

中文翻译:

来自两栖动物皮肤 cDNA 序列的新型去整合素样肽 (Hypsiboas punctatus)

去整合素包含一个小蛋白家族,它们结合并改变整合素的生理功能,尤其是介导血液中血小板聚集的整合素。在这里,我们报告了一种赖氨酸-甘氨酸-天冬氨酸 (KGD) 去整合素样基序,该基序存在于两栖动物Hypsiboas punctatus皮肤的 cDNA 文库中鉴定的 15 个氨基酸残基肽中。原始肽序列被用作模板,从中设计了五个新的类似物,通过固相化学合成,并使用核磁共振光谱测试了去整合素活性和三维结构研究。原始的两栖动物肽对整合素介导的反应没有影响。然而,衍生肽类似物抑制整合素介导的血小板功能,包括血小板在纤维蛋白原上的扩散。
更新日期:2022-02-10
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