Aggrekaanin

Aggrekaanin is a fictional protein used in theoretical biology to illustrate mechanisms of protein aggregation. It is not known to exist in nature but is used in teaching and modeling to explore how intrinsic disorder and aggregation-prone regions contribute to fibril formation.

Its described architecture is an intrinsically disordered protein of about 180 amino acids, enriched in glutamine and asparagine, with short hydrophobic motifs and no stable globular domain in its native state. Aggregation-prone regions are hypothesized to drive nucleation and promote beta-sheet–rich interfaces that seed fibril formation.

Under simulated physiological conditions and macromolecular crowding, aggrekaanin is predicted to undergo conformational rearrangements that yield amyloid-like fibrils, while in other conditions it remains soluble. Phase separation may produce dynamic condensates that concentrate aggregation-prone segments.

Research and education: Aggreakaanin is used in coursework and computational studies to illustrate how sequence features influence aggregation and to test algorithms for predicting aggregation propensity. Because aggreakaanin is not a real protein, there are no experimental measurements, structures, or biological roles assigned.

See also: amyloid, intrinsically disordered protein, prion-like domain, phase separation. References: This article describes a fictional construct; no empirical references exist.