(Gly22)-Amyloid beta-Protein (1-40) features a glycine substitution that shifts aggregation tendencies and oligomer formation. This alteration assists in pinpointing structural determinants of amyloid assembly. Its behavior in vitro aids studies on protein misfolding and aggregation energetics. The peptide is widely used in research focused on amyloidogenic processes and structural biology.
1. Urinary Metabolites Associated with Blood Pressure on a Low-or High-Sodium Die
2. Cationic cell-penetrating peptides are potent furin inhibitors
3. The spatiotemporal control of signalling and trafficking of the GLP-1R
4. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
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