{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Shi Y"],"funding":["National Institutes of Health","NIGMS NIH HHS","National Science Foundation"],"pagination":["12697-12706"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10484567"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["141(32)"],"pubmed_abstract":["Aggregation-induced emission (AIE) was intensively studied because of packing of small molecules and polymers; however, mid-molecular-weight (1000-3000) molecular scaffold containing a precise number of AIE luminogens is rare. Herein, we report the investigation of three tetraphenylethylene (TPE)-modified sulfono-γ-AApeptides in which multiple TPE moieties are conjugated to the chiral right-handed helical peptidomimetic backbone as functional side chains. The crystal structure of the TPE-α/sulfono-γ-AA peptide <b>1</b> demonstrates that because of the rigid helical scaffold of the TPE-α/sulfono-γ-AA peptides, the intramolecular rotations of the TPE with short linker are restricted, therefore leading to the boosted fluorescent emission in solution. Peptides <b>2</b> and <b>3</b> exhibit agg"],"journal":["Journal of the American Chemical Society"],"pubmed_title":["Helical Sulfono-γ-AApeptides with Aggregation-Induced Emission and Circularly Polarized Luminescence."],"pmcid":["PMC10484567"],"funding_grant_id":["R01 GM112652","1708500","1R01GM112652-01A1"],"pubmed_authors":["Wang M","Li X","Yin G","Zheng Y","Yan Z","Cai J","Sang P","Brzozowski R","Wojtas L","Eswara P","Shi Y"],"additional_accession":[]},"is_claimable":false,"name":"Helical Sulfono-γ-AApeptides with Aggregation-Induced Emission and Circularly Polarized Luminescence.","description":"Aggregation-induced emission (AIE) was intensively studied because of packing of small molecules and polymers; however, mid-molecular-weight (1000-3000) molecular scaffold containing a precise number of AIE luminogens is rare. Herein, we report the investigation of three tetraphenylethylene (TPE)-modified sulfono-γ-AApeptides in which multiple TPE moieties are conjugated to the chiral right-handed helical peptidomimetic backbone as functional side chains. The crystal structure of the TPE-α/sulfono-γ-AA peptide <b>1</b> demonstrates that because of the rigid helical scaffold of the TPE-α/sulfono-γ-AA peptides, the intramolecular rotations of the TPE with short linker are restricted, therefore leading to the boosted fluorescent emission in solution. Peptides <b>2</b> and <b>3</b> exhibit agg","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Aug","modification":"2025-05-29T19:51:15.618Z","creation":"2025-05-29T19:51:15.618Z"},"accession":"S-EPMC10484567","cross_references":{"pubmed":["31335135"],"doi":["10.1021/jacs.9b05329"]}}