| High-performance liquid chromatography after CuAAC initiation | Each combination showed an immediate decrease in the azido-peptide peak within the first 5 min and a new peak at higher retention time; monoexponential starting-material consumption; equilibrium conversion 35–60 %; all combinations reached equilibrium within approximately 20 min |
|---|---|
| DiO-C6 fluorescence after CuAAC initiation | C6- and C8-derived peptide amphiphiles assembled rapidly relative to C12-derived peptide amphiphiles; peptide-precursor alkyl-spacer length had negligible influence on assembly rates |
| Circular dichroism | Almost all derivatives showed a random-coil signature; P8C12 showed β-sheet character |
| Confocal fluorescence microscopy after 5 h | C6- and C8-based peptide amphiphiles showed isotropic colloidal morphology of micrometer-sized particles; P6C12 and P8C12 formed well-defined fibers with hierarchical bundling; P2C12 showed irregular architectures |
| Confocal fluorescence microscopy after 24 h | P2C12 transitioned into fiber bundles matching those of P6C12 and P8C12; fibrous morphology remained inaccessible to P2C6 and P2C8 after prolonged aging |
Nils Bäumer, Monika Wenisch, Ignacio Insua, Job Boekhoven. “Peptide amphiphile-based organelles for fueled synthetic cells.” ChemRxiv (). https://doi.org/10.26434/chemrxiv.15007627/v2
Values presented only in chromatographic, fluorescence, circular-dichroism, microscopy, photobleaching-recovery, and calorimetry plots or images were not transcribed. The main paper refers to supporting information, but no separate supporting information file was found among the files available from the ChemRxiv record
| High-performance liquid chromatography after centrifugation | Partitioning coefficients showed preferential accumulation of all peptide-amphiphile assemblies in the droplets, increasing gradually with tail length |
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| Fluorescence recovery after photobleaching, kinetically trapped state | Lower diffusivity than the control |
| Isothermal titration calorimetry, PSS binding | Binding to peptide-amphiphile assemblies was energetically more favorable per binding event than binding to activated peptide; the number of accessible binding sites was substantially lower; overall binding was less favorable than binding to activated peptide |