Proteeseille

Proteeseille is a hypothetical class of short, synthetic peptides conceived to act as modulators of protein homeostasis in cells. The term blends protein with a suffix that evokes small, seed-like entities. In the concept, proteeseilles are designed to interact with client proteins and proteostasis factors to influence folding, stability, or degradation.

Chemically, proteeseilles are characterized by flexible backbones and motifs that can tolerate proteolysis resistance, often incorporating noncanonical amino acids or D-amino acids, and bearing cationic or amphipathic features to engage chaperones or proteasome surfaces. They are typically produced by solid-phase peptide synthesis and can be engineered to bind specific targets or to act as generic modulators of the folding landscape.

Proposed mechanisms include transient stabilization of misfolded proteins, recruitment to degradation pathways, or acting as molecular glues between clients and chaperone complexes. Potential applications include studies of protein quality control, exploration of disease-related proteostasis defects, and the development of research tools for cell biology and drug discovery.

As a theoretical construct, proteeseille lacks confirmed in vivo demonstrations. Critics note challenges in achieving specificity, avoiding off-target effects, and delivering these agents into cells. Proponents place proteeseille discussions within broader efforts to understand proteostasis and to design molecules that can modulate protein turnover.