Compstatin Analogues Patent for Complement Inhibitors
Summary
USPTO granted patent US12600749B2 to ZP SPV 3 K/S on April 14, 2026, covering compstatin analogues with improved complement-inhibiting activity. The patent includes 19 claims for peptide variants with modifications at positions 3 and 9, as well as terminal sequences, providing improved binding affinity and solubility. Inventors include Anne Pernille Tofteng Shelton, Jacob Ulrik Fog, and Jens Kvist Madsen.
What changed
USPTO granted patent US12600749B2 to ZP SPV 3 K/S on April 14, 2026, covering compstatin analogues with improved complement-inhibiting activity. The patent claims variants with isoleucine at position 3, charged or polar amino acids at position 9, and modified N-/C-terminal sequences. The invention provides improved binding and solubility compared to the wild-type 13 amino acid compstatin peptide (ICVVQDWGHHRCT).
Pharmaceutical and biotech companies developing complement-targeted therapies should monitor this patent for potential freedom-to-operate implications. The 19 granted claims establish enforceable IP rights for the assignee. This is a routine patent grant providing IP protection—the therapeutic compounds themselves remain subject to separate regulatory approval processes before commercialization.
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Archived snapshot
Apr 14, 2026GovPing captured this document from the original source. If the source has since changed or been removed, this is the text as it existed at that time.
Compstatin analogues and their medical uses
Grant US12600749B2 Kind: B2 Apr 14, 2026
Assignee
ZP SPV 3 K/S
Inventors
Anne Pernille Tofteng Shelton, Jacob Ulrik Fog, Jens Kvist Madsen
Abstract
Compstatin analogues having improved binding and complement-inhibiting activity as compared to the 13 amino acid compstatin peptide (ICVVQDWGHHRCT (cyclic C2-C12)) (SEQ ID NO: 1) are described, in particular compstatin analogues that additionally possess useful physicochemical properties, such as increased solubility. These analogues include variants with an isoleucine residue at position 3 in place of the wild type valine residue, which provides compstatin peptides with improved binding and complement-inhibiting activity and also enables the introduction of other modifications, for example modifications that are capable of increasing solubility, such as the introduction of charged or polar amino acids at position 9 and/or the introduction of N- and/or C-terminal sequences.
CPC Classifications
C07K 7/08 A61K 47/542 A61K 38/00
Filing Date
2024-03-11
Application No.
18601031
Claims
19
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Source
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