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Cucurbit[7]uril Macrocyclic Sensors for Optical Fingerprinting: Predicting Protein Structural Changes to Identifying Disease-Specific Amyloid Assemblies.
Das Saha, Nilanjana; Pradhan, Soumen; Sasmal, Ranjan; Sarkar, Aritra; Berac, Christian M; Kölsch, Jonas C; Pahwa, Meenakshi; Show, Sushanta; Rozenholc, Yves; Topçu, Zeki; Alessandrini, Vivien; Guibourdenche, Jean; Tsatsaris, Vassilis; Gagey-Eilstein, Nathalie; Agasti, Sarit S.
Afiliación
  • Das Saha N; New Chemistry Unit, Jawaharlal Nehru Centre for Advanced Scientific Research (JNCASR), Bangalore, Karnataka 560064, India.
  • Pradhan S; Chemistry & Physics of Materials Unit, Jawaharlal Nehru Centre for Advanced Scientific Research (JNCASR), Bangalore, Karnataka 560064, India.
  • Sasmal R; Chemistry & Physics of Materials Unit, Jawaharlal Nehru Centre for Advanced Scientific Research (JNCASR), Bangalore, Karnataka 560064, India.
  • Sarkar A; New Chemistry Unit, Jawaharlal Nehru Centre for Advanced Scientific Research (JNCASR), Bangalore, Karnataka 560064, India.
  • Berac CM; New Chemistry Unit, Jawaharlal Nehru Centre for Advanced Scientific Research (JNCASR), Bangalore, Karnataka 560064, India.
  • Kölsch JC; Department of Chemistry, Johannes Gutenberg-University Mainz, Duesbergweg 10-14, 55128 Mainz, Germany.
  • Pahwa M; Graduate School of Materials Science in Mainz, Staudingerweg 9, 55128 Mainz, Germany.
  • Show S; Department of Chemistry, Johannes Gutenberg-University Mainz, Duesbergweg 10-14, 55128 Mainz, Germany.
  • Rozenholc Y; Chemistry & Physics of Materials Unit, Jawaharlal Nehru Centre for Advanced Scientific Research (JNCASR), Bangalore, Karnataka 560064, India.
  • Topçu Z; New Chemistry Unit, Jawaharlal Nehru Centre for Advanced Scientific Research (JNCASR), Bangalore, Karnataka 560064, India.
  • Alessandrini V; UR 7537 BioSTM, Université Paris Cité, 4 avenue de l'Observatoire, 75006 Paris, France.
  • Guibourdenche J; UR 7537 BioSTM, Université Paris Cité, 4 avenue de l'Observatoire, 75006 Paris, France.
  • Tsatsaris V; INSERM UMR-S 1139, Université Paris Cité, 4 avenue de l'Observatoire, 75006 Paris, France.
  • Gagey-Eilstein N; Department of Obstetrics, Cochin Hospital, AP-HP, Université Paris Cité, FHU PREMA, 123 Bd Port-Royal, 75014 Paris, France.
  • Agasti SS; INSERM UMR-S 1139, Université Paris Cité, 4 avenue de l'Observatoire, 75006 Paris, France.
J Am Chem Soc ; 144(31): 14363-14379, 2022 08 10.
Article en En | MEDLINE | ID: mdl-35913703
In a three-dimensional (3D) representation, each protein molecule displays a specific pattern of chemical and topological features, which are altered during its misfolding and aggregation pathway. Generating a recognizable fingerprint from such features could provide an enticing approach not only to identify these biomolecules but also to gain clues regarding their folding state and the occurrence of pathologically lethal misfolded aggregates. We report here a universal strategy to generate a fluorescent fingerprint from biomolecules by employing the pan-selective molecular recognition feature of a cucurbit[7]uril (CB[7]) macrocyclic receptor. We implemented a direct sensing strategy by covalently tethering CB[7] with a library of fluorescent reporters. When CB[7] recognizes the chemical and geometrical features of a biomolecule, it brings the tethered fluorophore into the vicinity, concomitantly reporting the nature of its binding microenvironment through a change in their optical signature. The photophysical properties of the fluorophores allow a multitude of probing modes, while their structural features provide additional binding diversity, generating a distinct fluorescence fingerprint from the biomolecule. We first used this strategy to rapidly discriminate a diverse range of protein analytes. The macrocyclic sensor was then applied to probe conformational changes in the protein structure and identify the formation of oligomeric and fibrillar species from misfolded proteins. Notably, the sensor system allowed us to differentiate between different self-assembled forms of the disease-specific amyloid-ß (Aß) aggregates and segregated them from other generic amyloid structures with a 100% identification accuracy. Ultimately, this sensor system predicted clinically relevant changes by fingerprinting serum samples from a cohort of pregnant women.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Hidrocarburos Aromáticos con Puentes / Péptidos beta-Amiloides Tipo de estudio: Prognostic_studies / Risk_factors_studies Límite: Female / Humans / Pregnancy Idioma: En Revista: J Am Chem Soc Año: 2022 Tipo del documento: Article País de afiliación: India Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Hidrocarburos Aromáticos con Puentes / Péptidos beta-Amiloides Tipo de estudio: Prognostic_studies / Risk_factors_studies Límite: Female / Humans / Pregnancy Idioma: En Revista: J Am Chem Soc Año: 2022 Tipo del documento: Article País de afiliación: India Pais de publicación: Estados Unidos