Amyndas has generated next-generation proprietary Compstatins with very significant improvements (18.000-fold) in binding affinity to human C3, enhanced inhibitory potency, and extended circulating in vivo half-life of >60 hr in pre-clinical models (e.g. AMY-101, AMY-201; KD 0.15 nM) compared with a much shorter half-life for earlier analogues (extensively reviewed in Mastellos et al., 2015, Qu et al., 2009, Ricklin and Lambris, 2008, Lamers et al., 2022, Mastellos et al., 2022.
In addition, Amyndas has developed compounds to target complement inhibition on cell surfaces by Compsorbin, which was first described by Dr. Lambris in 2011 (Wu et al. J. Immunology 186 (2011) 4269-77). Compsorbin is a fourteen amino acid cyclic peptide that binds to complement factor H and inhibits biomaterial and cell induced complement activation.
Moreover, Amyndas has developed compounds to target complement inhibition using factor H mini constructs which are 10x more active than earlier target complement inhibition compounds. Patents have been issued and U.S. and PCT patents have been filed for compositions of matter and methods of use for modulators of the complement cascade, and for development of products for the treatment of diseases and disorders with a major inflammatory component.
Amyndas has also developed proprietary compstatins sequences (e.g. Cp50) consisting exclusively of proteinogenic amino acids to enable their insertion into appropriate vectors for gene therapy applications. These next-generation compstatins are developed as stand-alone therapeutic entities or fusion constructs in combination with anti-VEGF (or other therapeutic modalities) for tissue-specific gene transduction and complement modulation in chronic inflammatory or immune-mediated diseases associated with prominent C3 dysregulation.
The company’s technology has also been evaluated in a number of high impact scientific publications and its lead candidates are increasingly recognized by the scientific community as the best C3 based complement inhibitors currently in development. For relevant publications, click here.