Valerio Guido Giacobelli

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 designs ancient proteins using a limited amino acid set and shows they are stable and mutation-resilient.

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.

This paper investigates the role of ribosomal peptides in protoribosome compartmentalization and stability, showing that RNA-protein interactions protect RNA from degradation and influence structural flexibility.