{"title":"DAPI(4',6-二氨基-2-苯基吲哚)作为淀粉样蛋白染色的一种新型荧光染料,与β-褶片结合。","authors":"Yu Uchida, Mao Mizukawa, Yumiko Kamiya, Takanori Shiga, Naoyuki Aihara, Junichi Kamiie","doi":"10.1080/10520295.2025.2552251","DOIUrl":null,"url":null,"abstract":"<p><p>Amyloidosis is caused by the extracellular deposition of amyloid fibrils with a β-pleated sheet structure. Diagnosis typically relies on Congo red or Thioflavine T staining. Recently, DAPI (4',6-Diamidino-2-Phenylindole), which is a common nuclear fluorochrome, has been reported to stain amyloid. DAPI staining is simpler than Congo Red and Thioflavine T staining, but its staining mechanism remains unclear. Thus, this study aimed to investigate the mechanism and specificity of DAPI staining for amyloid and its utility. The staining properties of DAPI and Thioflavine T for amyloid were compared on the basis of their stereochemical similarity. In addition, formic acid-treated amyloid specimens were used to investigate the mechanism by which structural changes affect DAPI binding to amyloid fibrils. DAPI staining was also evaluated in four specimens with different types of amyloid. DAPI and Thioflavine T had similar stereochemistry and staining behavior. The amyloid present in formic acid-treated specimens was negative for DAPI staining, indicating that DAPI may recognize the conformation of amyloid fibrils. DAPI stained positively in specimens deposited with AA, Aβ, AL, and AIAPP. DAPI staining recognizes the β-pleated sheet structure of the amyloid fibril structure, and is a simple and sensitive method for detecting amyloid deposition.</p>","PeriodicalId":8970,"journal":{"name":"Biotechnic & Histochemistry","volume":" ","pages":"1-10"},"PeriodicalIF":1.4000,"publicationDate":"2025-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"DAPI (4',6-diamidino-2-phenylindole) as a novel fluorochrome for amyloid staining that binds to β-pleated sheet.\",\"authors\":\"Yu Uchida, Mao Mizukawa, Yumiko Kamiya, Takanori Shiga, Naoyuki Aihara, Junichi Kamiie\",\"doi\":\"10.1080/10520295.2025.2552251\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Amyloidosis is caused by the extracellular deposition of amyloid fibrils with a β-pleated sheet structure. Diagnosis typically relies on Congo red or Thioflavine T staining. Recently, DAPI (4',6-Diamidino-2-Phenylindole), which is a common nuclear fluorochrome, has been reported to stain amyloid. DAPI staining is simpler than Congo Red and Thioflavine T staining, but its staining mechanism remains unclear. Thus, this study aimed to investigate the mechanism and specificity of DAPI staining for amyloid and its utility. The staining properties of DAPI and Thioflavine T for amyloid were compared on the basis of their stereochemical similarity. In addition, formic acid-treated amyloid specimens were used to investigate the mechanism by which structural changes affect DAPI binding to amyloid fibrils. DAPI staining was also evaluated in four specimens with different types of amyloid. DAPI and Thioflavine T had similar stereochemistry and staining behavior. The amyloid present in formic acid-treated specimens was negative for DAPI staining, indicating that DAPI may recognize the conformation of amyloid fibrils. DAPI stained positively in specimens deposited with AA, Aβ, AL, and AIAPP. DAPI staining recognizes the β-pleated sheet structure of the amyloid fibril structure, and is a simple and sensitive method for detecting amyloid deposition.</p>\",\"PeriodicalId\":8970,\"journal\":{\"name\":\"Biotechnic & Histochemistry\",\"volume\":\" \",\"pages\":\"1-10\"},\"PeriodicalIF\":1.4000,\"publicationDate\":\"2025-09-09\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biotechnic & Histochemistry\",\"FirstCategoryId\":\"5\",\"ListUrlMain\":\"https://doi.org/10.1080/10520295.2025.2552251\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q4\",\"JCRName\":\"BIOTECHNOLOGY & APPLIED MICROBIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biotechnic & Histochemistry","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1080/10520295.2025.2552251","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
DAPI (4',6-diamidino-2-phenylindole) as a novel fluorochrome for amyloid staining that binds to β-pleated sheet.
Amyloidosis is caused by the extracellular deposition of amyloid fibrils with a β-pleated sheet structure. Diagnosis typically relies on Congo red or Thioflavine T staining. Recently, DAPI (4',6-Diamidino-2-Phenylindole), which is a common nuclear fluorochrome, has been reported to stain amyloid. DAPI staining is simpler than Congo Red and Thioflavine T staining, but its staining mechanism remains unclear. Thus, this study aimed to investigate the mechanism and specificity of DAPI staining for amyloid and its utility. The staining properties of DAPI and Thioflavine T for amyloid were compared on the basis of their stereochemical similarity. In addition, formic acid-treated amyloid specimens were used to investigate the mechanism by which structural changes affect DAPI binding to amyloid fibrils. DAPI staining was also evaluated in four specimens with different types of amyloid. DAPI and Thioflavine T had similar stereochemistry and staining behavior. The amyloid present in formic acid-treated specimens was negative for DAPI staining, indicating that DAPI may recognize the conformation of amyloid fibrils. DAPI stained positively in specimens deposited with AA, Aβ, AL, and AIAPP. DAPI staining recognizes the β-pleated sheet structure of the amyloid fibril structure, and is a simple and sensitive method for detecting amyloid deposition.
期刊介绍:
Biotechnic & Histochemistry (formerly Stain technology) is the
official publication of the Biological Stain Commission. The journal has been in continuous publication since 1926.
Biotechnic & Histochemistry is an interdisciplinary journal that embraces all aspects of techniques for visualizing biological processes and entities in cells, tissues and organisms; papers that describe experimental work that employs such investigative methods are appropriate for publication as well.
Papers concerning topics as diverse as applications of histochemistry, immunohistochemistry, in situ hybridization, cytochemical probes, autoradiography, light and electron microscopy, tissue culture, in vivo and in vitro studies, image analysis, cytogenetics, automation or computerization of investigative procedures and other investigative approaches are appropriate for publication regardless of their length. Letters to the Editor and review articles concerning topics of special and current interest also are welcome.