Additional file 1 of The protein aggregation inhibitor YAT2150 has potent antimalarial activity in Plasmodium falciparum in vitro cultures
Creators: name: Bouzón-Arnáiz, Inés
name: Avalos-Padilla, Yunuen
name: Biosca, Arnau
name: Caño-Prades, Omar
name: Román-Álamo, Lucía
name: Valle, Javier
name: Andreu, David
name: Moita, Diana
name: Prudêncio, Miguel
name: Arce, Elsa M.
name: Muñoz-Torrero, Diego
name: Fernàndez-Busquets, Xavier
Publisher: name: figshare
Year: 2022
Subjects: subject: Biochemistry
subject: 29999 Physical Sciences not elsewhere classified
subject: FOS: Physical sciences
subject: Medicine
subject: Microbiology
subject: FOS: Biological sciences
subject: Cell Biology
subject: Genetics
subject: Pharmacology
subject: Biotechnology
subject: Cancer
subject: 110309 Infectious Diseases
subject: FOS: Health sciences

description: Additional file 1: Figures S1-S12 and Tables S1-S9. Figure S1. Analysis of the aggregation of six peptides present in P. falciparum proteins. Figure S2. Flow cytometry analysis of the colocalization with RBCs and pRBCs of fluorescein-labeled LMWP-conjugated peptides. Figure S3. Flow cytometry analysis of the colocalization with RBCs and pRBCs of fluorescein-labeled TAT-conjugated peptides. Figure S4. Flow cytometry analysis of the colocalization with RBCs and pRBCs of fluorescein-labeled TP2-conjugated peptides. Figure S5. Flow cytometry analysis of the parasitemia, 72 h post-infection, in P. falciparum cultures grown in regular and ghost RBCs. Figure S6. Aggregative proteins found in late and early P. falciparum blood stages represented according to their abundance and aggregation propensity normalized relative to the whole proteome. Figure S7. In vitro analysis of the aggregation of KDLLF, KVVNI and derived peptides. Figure S8. Confocal fluorescence microscopy analysis of the presence of the fluorescein-labeled peptides KDLLF and KVVNI, and of their LMWP elongations, in ghost pRBCs. Figure S9. Effect of YAT2150 on pre-aggregated Aβ40. Figure S10. ThT analysis of the effect of YAT2150 on the in vitro aggregation of aggregative peptides present in P. falciparum proteins. Figure S11. Determination of protein aggregation in live P. falciparum cultures. Figure S12. Hemozoin formation assay. Table S1. Aggregative peptides selected from the pool of 369 proteins resisting dissolution in 0.1% SDS identified in Biosca et al., 2020. Table S2. Growth inhibition assay in regular P. falciparum cultures of fluorescein-labeled aggregative peptides conjugated to CPPs. Table S3. Growth inhibition assay in ghost RBC-enriched P. falciparum cultures treated with 10 µM non-modified aggregative peptides. Table S4. Cytotoxicity assay in HUVEC cultures of the aggregative peptides which at 10 µM reduced by &gt; 20% P. falciparum growth in ghost pRBC cultures. Table S5. Early stage P. falciparum proteins resisting dissolution in 0.1% SDS. Table S6. Aggregative peptides identified in P. falciparum E3 ubiquitin-protein ligase (C0H4K6). Table S7. P. falciparum proteins in which the peptides KDLLF and KVVNI are present. Table S8. Growth inhibition assay in ghost RBC-enriched P. falciparum cultures treated with 10 µM KDLLF and KVVNI peptides. Table S9. In vitro toxicity in HUVEC cultures of amyloid pan-inhibitors.