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SAP 22mer is a synthetic 22-amino acid peptide derived from the N-terminal region (residues 1-22) of the human Serum Amyloid P component (SAP). Developed primarily by researchers at the University of Tennessee, this peptide is designed to exploit the natural affinity of the SAP protein for amyloid fibrils. SAP 22mer specifically binds to the cross-beta sheet quaternary structure common to all types of amyloid deposits, including AL, ATTR, and Aβ, making it a pan-amyloid targeting agent. While it has been extensively studied in preclinical models as a radiotracer for PET and SPECT imaging of systemic amyloidosis, it also serves as a molecular scaffold for the development of therapeutic agents aimed at disrupting fibril stability or delivering localized immunotherapy. Its development has led to more potent synthetic derivatives, such as the p5 and p5+14 peptides, which have progressed further into clinical evaluation.
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