Kaito Hayakawa, Masaya Hane, Hiroki Hamagami, Miki Imai, Hiroshi Tanaka, Ken Kitajima, Chihiro Sato
{"title":"聚唾液酸和多巴胺铅化合物之间的相互作用揭示了生化和硅对接模拟分析。","authors":"Kaito Hayakawa, Masaya Hane, Hiroki Hamagami, Miki Imai, Hiroshi Tanaka, Ken Kitajima, Chihiro Sato","doi":"10.1007/s10719-023-10119-6","DOIUrl":null,"url":null,"abstract":"<p><p>Polysialic acid is an important glyco-epitope in vertebrate brains, while altered expressions of polySia and biosynthetic enzyme have been reported in brain diseases such as schizophrenia and depression. Recently, the binding between polySia and dopamine and the involvement of this in Akt signaling has been demonstrated. However, the molecular mechanism underlying the binding of polySia and dopamine remains unknown. Therefore, here, we demonstrated the interaction between dopamine and polySia using frontal affinity chromatography alongside docking simulations. In addition, we prepared dopamine-lead compounds to understand the detailed molecular basis of polySia binding by frontal affinity chromatography, enzyme-linked immunosorbent assay, and docking simulations.</p>","PeriodicalId":12762,"journal":{"name":"Glycoconjugate Journal","volume":"40 4","pages":"461-471"},"PeriodicalIF":2.7000,"publicationDate":"2023-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Interactions between polysialic acid and dopamine-lead compounds as revealed by biochemical and in silico docking simulation analyses.\",\"authors\":\"Kaito Hayakawa, Masaya Hane, Hiroki Hamagami, Miki Imai, Hiroshi Tanaka, Ken Kitajima, Chihiro Sato\",\"doi\":\"10.1007/s10719-023-10119-6\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Polysialic acid is an important glyco-epitope in vertebrate brains, while altered expressions of polySia and biosynthetic enzyme have been reported in brain diseases such as schizophrenia and depression. Recently, the binding between polySia and dopamine and the involvement of this in Akt signaling has been demonstrated. However, the molecular mechanism underlying the binding of polySia and dopamine remains unknown. Therefore, here, we demonstrated the interaction between dopamine and polySia using frontal affinity chromatography alongside docking simulations. In addition, we prepared dopamine-lead compounds to understand the detailed molecular basis of polySia binding by frontal affinity chromatography, enzyme-linked immunosorbent assay, and docking simulations.</p>\",\"PeriodicalId\":12762,\"journal\":{\"name\":\"Glycoconjugate Journal\",\"volume\":\"40 4\",\"pages\":\"461-471\"},\"PeriodicalIF\":2.7000,\"publicationDate\":\"2023-08-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Glycoconjugate Journal\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1007/s10719-023-10119-6\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Glycoconjugate Journal","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1007/s10719-023-10119-6","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
Interactions between polysialic acid and dopamine-lead compounds as revealed by biochemical and in silico docking simulation analyses.
Polysialic acid is an important glyco-epitope in vertebrate brains, while altered expressions of polySia and biosynthetic enzyme have been reported in brain diseases such as schizophrenia and depression. Recently, the binding between polySia and dopamine and the involvement of this in Akt signaling has been demonstrated. However, the molecular mechanism underlying the binding of polySia and dopamine remains unknown. Therefore, here, we demonstrated the interaction between dopamine and polySia using frontal affinity chromatography alongside docking simulations. In addition, we prepared dopamine-lead compounds to understand the detailed molecular basis of polySia binding by frontal affinity chromatography, enzyme-linked immunosorbent assay, and docking simulations.
期刊介绍:
Glycoconjugate Journal publishes articles and reviews on all areas concerned with:
function, composition, structure, biosynthesis, degradation, interactions, recognition and chemo-enzymatic synthesis of glycoconjugates (glycoproteins, glycolipids, oligosaccharides, polysaccharides and proteoglycans), biochemistry, molecular biology, biotechnology, immunology and cell biology of glycoconjugates, aspects related to disease processes (immunological, inflammatory, arthritic infections, metabolic disorders, malignancy, neurological disorders), structural and functional glycomics, glycoimmunology, glycovaccines, organic synthesis of glycoconjugates and the development of methodologies if biologically relevant, glycosylation changes in disease if focused on either the discovery of a novel disease marker or the improved understanding of some basic pathological mechanism, articles on the effects of toxicological agents (alcohol, tobacco, narcotics, environmental agents) on glycosylation, and the use of glycotherapeutics.
Glycoconjugate Journal is the official journal of the International Glycoconjugate Organization, which is responsible for organizing the biennial International Symposia on Glycoconjugates.