<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>7(16)</volume><submitter>Dave R</submitter><pubmed_abstract>This study expands the platform for amyloidogenic building blocks, such as nucleobases, and their self-assembly. Here, we examine the self-assembly profile of nucleobases such as guanine, cytosine, and thymine and determine that these nucleobases, while aged, produce small globules which gradually transform into fibrillar assemblies. Notably, the amyloid-like fibrillation in adenine and uracil has already been reported; hence, it was imperative to understand the amyloidogenic propensity in these unexplored nucleobases. The aggregates formed by guanine, cytosine, and thymine interestingly reveal a distinctive spectrum characteristic of amyloidogenic proteins after binding to the amyloid-specific dye Thioflavin T (ThT). The MTT assay in human retinal pigment epithelial RPE-1 cell lines revea</pubmed_abstract><journal>Nanoscale advances</journal><pagination>5093-5103</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12258404</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Nucleobase self-assembly: aggregation, morphological characterization, and toxicity analysis.</pubmed_title><pmcid>PMC12258404</pmcid><pubmed_authors>Verma S</pubmed_authors><pubmed_authors>Jaiswal A</pubmed_authors><pubmed_authors>Nazir A</pubmed_authors><pubmed_authors>Naseer A</pubmed_authors><pubmed_authors>Gour N</pubmed_authors><pubmed_authors>Dave R</pubmed_authors><pubmed_authors>Singh A</pubmed_authors><pubmed_authors>Bhatia D</pubmed_authors><pubmed_authors>Patel M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Nucleobase self-assembly: aggregation, morphological characterization, and toxicity analysis.</name><description>This study expands the platform for amyloidogenic building blocks, such as nucleobases, and their self-assembly. Here, we examine the self-assembly profile of nucleobases such as guanine, cytosine, and thymine and determine that these nucleobases, while aged, produce small globules which gradually transform into fibrillar assemblies. Notably, the amyloid-like fibrillation in adenine and uracil has already been reported; hence, it was imperative to understand the amyloidogenic propensity in these unexplored nucleobases. The aggregates formed by guanine, cytosine, and thymine interestingly reveal a distinctive spectrum characteristic of amyloidogenic proteins after binding to the amyloid-specific dye Thioflavin T (ThT). The MTT assay in human retinal pigment epithelial RPE-1 cell lines revea</description><dates><release>2025-01-01T00:00:00Z</release><publication>2025 Aug</publication><modification>2026-03-31T11:48:54.044Z</modification><creation>2025-09-01T03:05:54.375Z</creation></dates><accession>S-EPMC12258404</accession><cross_references><pubmed>40666605</pubmed><doi>10.1039/d5na00259a</doi></cross_references></HashMap>