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Product News

Long-Acting Peptide Therapy for Heart Failure To Be Developed by AL-Protein and Bioscience

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Product News

Long-Acting Peptide Therapy for Heart Failure To Be Developed by AL-Protein and Bioscience

Credit: Joshua Coleman/ Unsplash

Antlia Bioscience, Inc., a privately owned biopharmaceutical company located in San Diego, California, and XL-protein GmbH, a privately owned biopharmaceutical company located in Germany, are pleased to announce a strategic slliance using XL-protein's proprietary PASylation® technology for plasma half-life extension to develop a novel, long-acting, peptide therapeutic treatment for chronic heart failure. Brian Johnson, Antlia Bioscience’s CEO commented, "chronic heart failure is a significantly unaddressed medical condition and a major public health concern. XL-protein's PASylation® technology will allow us to safely and effectively translate our peptide into a meaningful therapeutic option for patients with chronic heart failure. "PASylation® is an excellent biological solution for plasma-half extension of therapeutic peptides, and we believe that PASylation® offers a simpler manufacturing process and superior pharmacological properties," commented Claus Schalper, CEO of XL-protein. "We are excited to work with Antlia Bioscience to further exploit the potential of our technology and to develop new therapeutic options for the treatment of chronic heart failure." Financial terms of the agreement have not been disclosed.

About PASylation® Technology

'PASylation' involves the genetic fusion or chemical conjugation of a therapeutic protein or pharmaceutically active compound with a conformationally disordered polypeptide of defined sequence comprising the small natural amino acids Pro, Ala, and/or Ser. Due to the biophysical size effect, the typically rapid clearance via renal filtration of the original drug can be retarded by a factor 10-100, depending on the length of the PAS chain. PAS sequences are highly soluble while lacking charges, they are biochemically inert, non-toxic and non-immunogenic, they offer efficient recombinant protein production in a variety of biotechnological host organisms, and they show high stability in blood plasma but are biodegradable by intracellular proteases.


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