{"created":"2023-06-20T16:36:17.728186+00:00","id":5793,"links":{},"metadata":{"_buckets":{"deposit":"d0275e1c-540f-41f2-83f1-48d5eb11697b"},"_deposit":{"created_by":3,"id":"5793","owners":[3],"pid":{"revision_id":0,"type":"depid","value":"5793"},"status":"published"},"_oai":{"id":"oai:kindai.repo.nii.ac.jp:00005793","sets":["14:923:1549:1550","21:3039:3109:3145"]},"author_link":["8889","8890"],"item_2_alternative_title_3":{"attribute_name":"その他（別言語等）のタイトル","attribute_value_mlt":[{"subitem_alternative_title":"天然ジスルフィド結合によるミスフォールディングとアミロイド線維形成の増進"}]},"item_2_biblio_info_21":{"attribute_name":"書誌情報","attribute_value_mlt":[{"bibliographicIssueDates":{"bibliographicIssueDate":"2015-09-01","bibliographicIssueDateType":"Issued"},"bibliographicPageEnd":"26","bibliographicPageStart":"19","bibliographicVolumeNumber":"36","bibliographic_titles":[{"bibliographic_title":"近畿大学生物理工学部紀要"},{"bibliographic_title":"Memoirs of the Faculty of Biology-Oriented Science and Technology of Kinki University","bibliographic_titleLang":"en"}]}]},"item_2_description_33":{"attribute_name":"抄録","attribute_value_mlt":[{"subitem_description":"[Abstract] Native disulfide bonds are generally thought to assist correct folding, and therefore to depress misfolding. Here, the effect of the presence of individual disulfide bonds on the amyloid fibrillation of hen lysozyme was investigated by using a set of disulfide-variant proteins: 0SS, an all-disulfide-deficient variant; 1SS, single-disulfide variants; 2SS, double-disulfide variants; 3SS, triple-disulfide variants; and 4SS (WT). The protein conformation in a monomeric state covered by this set of variants ranges from global unfolding, through various local folding, to a global folding. Under the solution conditions not favoring spontaneous fibrillation, seeded fibrillation reactions were carried out using sonicated WT lysozyme fibril fragments as seeds and the disulfide variants as reactants for fibril-elongation, and monitored with thioflavine T fluorescence, CD spectroscopy, and scanning probe microscopy. Contrary to the general expectation, disulfide bonds C64-C80 and C76-C94 enhanced amyloid-fibrillation indicating that these native disulfide bonds have a positive role in the misfolding into regular intermolecular β-structures and fibrillation. The other native disulfide bonds C6-C127 and C30-C115 depressed the fibrillation reaction.　　　　　　　　　　　　　　　　　　　　[要旨] 天然状態の蛋白質に見られるジスルフィド結合は正しいフォールディングを助長し, ミスフォールディングを抑制すると一般に考えられている. ここに報告する研究では, 一連のジスルフィド結合変異体を用いて, ニワトリリゾチームのアミロイド線維化に及ぼすジスルフィド結合の効果を調ベた. これらの変異体は, 全てのジスルフィド結合を欠損したもの(0SS),  1個のジスルフィド結合を保持したもの(1SS), 2個のジスルフィド結合を保持したもの(2SS),  3個のジスルフィド結合を保持したもの(3SS), そして4個のジスルフィド結合を保持したもの(これは野生型蛋白に相当)である. これらの変異体は, 単一分子状態での蛋白質コンフォメーションとして, 全体的にアンフォールドした状態, 色々な部位が局所的にフォールドした状態, そして全体がフォールドした状態を網羅する. 自発的線維化反応が起こりにくい溶液条件下において, 野生型リゾチームアミロイド線維を超音波処理によって断片化したものを種として上記の色々なジスルフィド結合変異体を付加 ・伸長させる「種由来線維化反応」を行い, チオフラヴィン T蛍光, 円二色性分光, 走査探針顕微鏡によってモニターした. その結果, 一般的な予測に反し, ジスルフイド結合 C64-C80 ならびに C76-C94 はアミロイド線維化反応を増進する, 即ち, これらの天然のジスルフィド結合は規則的な分子間β構造ヘのミスフォールディング, そして線維形成を促進する役割を持つことがわかった. 一方, 他の2本の天然のジスルフィド結合C6-C127およびC30-C115は線維化反応を低下させることが示された.","subitem_description_type":"Abstract"}]},"item_2_description_41":{"attribute_name":"フォーマット","attribute_value_mlt":[{"subitem_description":"application/pdf","subitem_description_type":"Other"}]},"item_2_publisher_14":{"attribute_name":"出版者 名前","attribute_value_mlt":[{"subitem_publisher":"近畿大学生物理工学部"}]},"item_2_source_id_22":{"attribute_name":"ISSN","attribute_value_mlt":[{"subitem_source_identifier":"13427202","subitem_source_identifier_type":"ISSN"}]},"item_2_text_7":{"attribute_name":"著者(英)","attribute_value_mlt":[{"subitem_text_language":"en","subitem_text_value":"橘, 秀樹"},{"subitem_text_language":"en","subitem_text_value":"河野, 良平"}]},"item_2_text_8":{"attribute_name":"著者 所属","attribute_value_mlt":[{"subitem_text_value":"近畿大学生物理工学部生物工学科: 近畿大学先端技術総合研究所高圧力蛋白質研究センター"},{"subitem_text_value":"和歌山県立医科大学機能性医薬食品探索講座"}]},"item_2_text_9":{"attribute_name":"著者所属(翻訳)","attribute_value_mlt":[{"subitem_text_value":"Department of Biotechnological Science, Kinki University: High Pressure Protein Research Center, Institute of Advanced Technology, Kinki Univertsity"},{"subitem_text_value":"Department of Strategic Surveillance for Functional Food and Comprehensive Traditional Medicine, Wakayama Medical University"}]},"item_2_version_type_12":{"attribute_name":"版","attribute_value_mlt":[{"subitem_version_resource":"http://purl.org/coar/version/c_970fb48d4fbd8a85","subitem_version_type":"VoR"}]},"item_creator":{"attribute_name":"著者","attribute_type":"creator","attribute_value_mlt":[{"creatorNames":[{"creatorName":"Tachibana,  Hideki"},{"creatorName":"タチバナ, ヒデキ","creatorNameLang":"ja-Kana"}],"nameIdentifiers":[{}]},{"creatorNames":[{"creatorName":"Kono,  Ryohei"},{"creatorName":"コウノ, リョウヘイ","creatorNameLang":"ja-Kana"}],"nameIdentifiers":[{}]}]},"item_files":{"attribute_name":"ファイル情報","attribute_type":"file","attribute_value_mlt":[{"accessrole":"open_date","date":[{"dateType":"Available","dateValue":"2016-02-18"}],"displaytype":"detail","filename":"AN1153712-20150930-0019.pdf","filesize":[{"value":"7.4 MB"}],"format":"application/pdf","licensetype":"license_note","mimetype":"application/pdf","url":{"label":"AN1153712-20150930-0019.pdf","url":"https://kindai.repo.nii.ac.jp/record/5793/files/AN1153712-20150930-0019.pdf"},"version_id":"23d30315-73a1-4983-8cef-26ae43264b55"}]},"item_keyword":{"attribute_name":"キーワード","attribute_value_mlt":[{"subitem_subject":"アミロイド線維化","subitem_subject_scheme":"Other"},{"subitem_subject":"ジスルフィド結合","subitem_subject_scheme":"Other"},{"subitem_subject":"蛋白質のミスフォールディング","subitem_subject_scheme":"Other"},{"subitem_subject":"リゾチーム変異体","subitem_subject_scheme":"Other"},{"subitem_subject":"amyloid fibrillation","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"disulfide bond","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"protein misfolding","subitem_subject_language":"en","subitem_subject_scheme":"Other"},{"subitem_subject":"lysozyme variant","subitem_subject_language":"en","subitem_subject_scheme":"Other"}]},"item_language":{"attribute_name":"言語","attribute_value_mlt":[{"subitem_language":"eng"}]},"item_resource_type":{"attribute_name":"資源タイプ","attribute_value_mlt":[{"resourcetype":"departmental bulletin paper","resourceuri":"http://purl.org/coar/resource_type/c_6501"}]},"item_title":"〈Original Papers〉Enhancement of Misfolding and Amyloid Fibrillation by Native Disulfide Bonds","item_titles":{"attribute_name":"タイトル","attribute_value_mlt":[{"subitem_title":"〈Original Papers〉Enhancement of Misfolding and Amyloid Fibrillation by Native Disulfide Bonds","subitem_title_language":"en"}]},"item_type_id":"2","owner":"3","path":["1550","3145"],"pubdate":{"attribute_name":"公開日","attribute_value":"2015-12-10"},"publish_date":"2015-12-10","publish_status":"0","recid":"5793","relation_version_is_last":true,"title":["〈Original Papers〉Enhancement of Misfolding and Amyloid Fibrillation by Native Disulfide Bonds"],"weko_creator_id":"3","weko_shared_id":3},"updated":"2023-06-20T19:19:43.747155+00:00"}