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The conformation and dynamics of intercalated DNA and nucleosome analyzed by molecular dynamics simulation
https://repo.qst.go.jp/records/2002103
https://repo.qst.go.jp/records/2002103fb1a6050-9dbf-4ff1-83c1-bafb0e3f7382
| アイテムタイプ | 会議発表用資料 / Presentation(1) | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| 公開日 | 2025-09-29 | |||||||||
| タイトル | ||||||||||
| タイトル | The conformation and dynamics of intercalated DNA and nucleosome analyzed by molecular dynamics simulation | |||||||||
| 言語 | en | |||||||||
| 言語 | ||||||||||
| 言語 | eng | |||||||||
| 資源タイプ | ||||||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_c94f | |||||||||
| 資源タイプ | conference presentation | |||||||||
| 著者 |
Ishida Hisashi
× Ishida Hisashi
× Kono Hidetoshi
|
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| 抄録 | ||||||||||
| 内容記述 | Intercalators modulate DNA structure through direct molecular interactions, influencing replication and transcription. Using molecular dynamics simulations with 18-mer DNA, we investigated binding mechanisms of SYBR Gold, YOYO-1, and DOXO (doxorubicin). Two primary intercalation patterns were observed: insertion between adjacent base pairs (RISE-type) and insertion via base-pair opening (OPEN-type). These interaction modes distinctly altered DNA contour length and stiffness. Further investigating DOXO in a nucleosome system revealed preferential binding to nucleosomal DNA , which reduced atomic contacts between DNA and histone arginine residues, potentially destabilizing nucleosome structure and facilitating histone eviction. | |||||||||
| 会議概要（会議名, 開催地, 会期, 主催者等） | ||||||||||
| 内容記述 | 第63回日本生物物理学会年会 | |||||||||
| 発表年月日 | ||||||||||
| 日付 | 2025-09-24 | |||||||||
