Robin Kryštůfek

This study compares how different cationic chemistries influence peptide-RNA coacervation, showing that statistical peptide ensembles can drive protoribosomal condensate formation without sequence-specific optimization.

The paper shows that peptides made from non-standard amino acids can form protein-like secondary structures, expanding the known sequence-structure space beyond Earth's 20 amino acids.

This study shows random 25-mer peptides with a prebiotically plausible amino acid alphabet can self-assemble into thermostable beta-rich nanostructures.

This study investigates how peptides interact with mineral surfaces and lipid vesicles, showing acidic residues bind minerals and arginine enhances phosphate mobilization, while different amino acid alphabets affect vesicle stability.

The paper presents a qPCR-based method for high-throughput screening of FDA-approved compounds as FAP inhibitors and demonstrates its application in quantifying FAP in human plasma.