Attralus to Present New Data on Its Amyloidosis Portfolio at the 2022 International Symposium on Amyloidosis

SAN FRANCISCO, Aug. 22, 2022 (GLOBE NEWSWIRE) -- Attralus, Inc., a clinical stage biopharmaceutical company developing transformative medicines to improve the lives of patients with systemic amyloidosis, today announced that new data across the Company's amyloidosis portfolio will be presented in both oral and poster presentations at the XVIII International Symposium on Amyloidosis (ISA) by Attralus, the University of Tennessee Graduate School of Medicine and the Brigham and Women's Hospital. The Company will also be hosting a satellite symposium on Thursday, September 8, 2022. ISA is taking place September 4-8, 2022, in Heidelberg, Germany, presented by the International Society of Amyloidosis.

“Systemic amyloidosis is a group of progressive and debilitating diseases that are a challenge for both diagnosis and treatment. Diagnosis can take years and, while therapies exist to slow, or even stop, the accumulation of toxic amyloid, there are no available therapies to remove amyloid from patients,” said Gregory Bell, M.D., Chief Medical Officer of Attralus. “At ISA, we will present data across our portfolio of pan-amyloid removal (PAR) therapeutics and the first and only non-invasive, pan-amyloid PET imaging agent designed to detect all types of systemic amyloidosis. We are excited to be able to share these data at the International Symposium on Amyloidosis.”

Oral Presentation Details

Abstract Title: Pan-amyloid reactivity of radioiodinated peptide 124I-AT-01 in patients with systemic amyloidosis demonstrated by PET/CT imaging

  • Presented by: Emily Martin, Ph.D., Assistant Professor, University of Tennessee Graduate School of Medicine
  • Session: 3. Scientific Session: Imaging in Amyloidosis
  • Date/Time: September 5, 2022, 1:25 p.m. – 3:05 p.m. CEST

Abstract Title: Results of the first-in-human PET/CT imaging study of the amyloid-reactive peptide 124I-AT-01(124I-p5+14) for the detection of systemic amyloidosis

  • Presented by: Jonathan Wall, Ph.D., Distinguished Professor and Director of the University of Tennessee Graduate School of Medicine’s Amyloidosis and Cancer Theranostics Program Session: 3. Scientific Session: Imaging in Amyloidosis
  • Date/Time: September 5, 2022, 1:25 p.m. – 3:05 p.m. CEST

Abstract Title: Preclinical characterization of AT-02, a pan-amyloid-binding immunoglobulin-peptide fusion protein capable of inducing enhanced phagocytosis of amyloid

  • Presented by: Jonathan Wall, Ph.D., Distinguished Professor and Director of the University of Tennessee Graduate School of Medicine’s Amyloidosis and Cancer Theranostics Program Session: 6. Scientific Session: Basic Research - New Treatment Targets and Biomarkers
  • Date/Time: September 6, 2022, 10:30 a.m. – 12:05 p.m. CEST

Abstract Title: Development of novel human chimeric antigen receptor-macrophages (CAR-M) as a potential therapeutic for amyloid clearance

  • Presented by: Manasi Balachandran, Ph.D., Assistant Professor, University of Tennessee Graduate School of Medicine
  • Session: 6. Scientific Session: Basic Research - New Treatment Targets and Biomarkers
  • Date/Time: September 6, 2022, 10:30 a.m. – 12:05 p.m. CEST

Satellite Symposium Details

Topic: Unmet Need and Rationale for Anti-Amyloid Therapy in Systemic Amyloidosis

  • Moderated by: Ashutosh Wechalekar, M.D., University College London
  • Speakers:
    • Morie Gertz, M.D., Mayo Clinic
    • Marina Ramirez-Alvarado, Ph.D., Mayo Clinic
    • Arnt Kristen, M.D., University Hospital Heidelberg (Universitätsklinikum Heidelberg)
  • Date/Time: September 8, 2022, 7:45 a.m. – 8:30 a.m. CEST
  • Location: Hall 14, Neue Universität and online

Poster Presentation Details

  • Poster P187: Quantification of left ventricular amyloid using 124I-p5+14 (AT-01) and 18F-florbetapir positron emission tomography in AL and ATTR amyloidosis
    • Presented by: Olivier Clerc, M.D., M.P.H., Research Fellow Amyloidosis Program, Brigham and Women's Hospital
    • Date/Time: September 6, 2022, 12:05 p.m. – 1:15 p.m. CEST
  • Poster P169: Differentiation of ATTR amyloidosis based on abdominothoracic organ-specific uptake of 124I-AT-01 (124I-p5+14) assessed by PET/CT imaging
    • Presented by: R. Eric Heidel, Ph.D., Associate Professor, University of Tennessee Graduate School of Medicine
    • Date/Time: September 6, 2022, 12:05 p.m. – 1:15 p.m. CEST
  • Poster P163: A kit method for direct radiolabeling the amyloid reactive peptide p5+14 with technetium-99m (99mTc) for the detection of cardiac amyloidosis by SPECT/CT imaging
    • Presented by: Stephen J. Kennel, Ph.D., Professor, University of Tennessee Graduate School of Medicine
    • Date/Time: September 6, 2022, 12:05 p.m. – 1:15 p.m. CEST
  • Poster P164: Quantitative changes in organ-specific amyloid load in a patient with AL amyloidosis, measured by 124I-AT-01 PET/CT imaging, correlate with serum biomarkers
    • Presented by: Alan Stuckey, C.N.M.T., Research Director, University of Tennessee Graduate School of Medicine
    • Date/Time: September 6, 2022, 12:05 p.m. – 1:15 p.m. CEST
  • Poster P170: Detection of extracardiac amyloid in patients with ATTR amyloidosis by PET/CT imaging using the amyloidophilic radiotracer 124I-AT-01 (124I-p5+14)
    • Presented by: Jonathan Wall, Ph.D., Distinguished Professor and Director of the University of Tennessee Graduate School of Medicine’s Amyloidosis and Cancer Theranostics Program
    • Date/Time: September 6, 2022, 12:05 p.m. – 1:15 p.m. CEST
  • Poster P284: AT-03 demonstrated pan-amyloid binding and stimulated the removal of amyloid deposits through Macrophage-mediated phagocytosis
    • Presented by: Christophe Sirac, Ph.D., Professor, University of Limoges
    • Date/Time: September 7, 2022, 12:05 p.m. – 1:20 p.m. CEST
  • Poster P282: Preclinical characterization of AT-04, a pan-amyloid-binding Fc domain-peptide fusion, to serve as an opsonin for macrophage-mediated clearance of amyloid deposits
    • Presented by: J. Steve Foster, M.S., Research Associate, University of Tennessee Graduate School of Medicine
    • Date/Time: September 7, 2022, 12:05 p.m. – 1:20 p.m. CEST

For additional information, please visit the ISA 2022 website.

About Systemic Amyloidosis 

Systemic amyloidosis encompasses a diverse group of rare diseases that occur due to accumulation of toxic amyloid deposits in tissues and organs, a consequence of aberrant protein misfolding events. These diseases are progressive, debilitating and often fatal. Systemic amyloidosis is significantly underdiagnosed due to low awareness, lack of specific symptoms, and no current disease-specific diagnostics. The two most common forms of systemic amyloidosis are immunoglobulin light-chain-associated (AL) amyloidosis and transthyretin-associated amyloidosis (ATTR). There is a significant unmet need for new therapies and diagnostics in systemic amyloidosis. 

About AT-01 Pan-Amyloid Diagnostic

AT-01 (iodine-124 Evuzamitide) utilizes the company’s pan-amyloid binding peptide as an amyloid-specific imaging agent to image all types of systemic amyloidosis by PET/CT imaging. In initial clinical trials, AT-01 has been shown to detect multiple types of amyloid deposits, including AL and ATTR, in major organs such as the heart, kidney, liver and spleen. Attralus obtained exclusive rights to commercialize AT-01 under a commercial license agreement with the University of Tennessee Research Foundation. The same PAR-peptide technology is utilized in AT-02 and AT-04, two of the company’s therapeutic candidates.

About AT-02 PAR Therapeutic

AT-02 is a fusion of our PAR-peptide technology with an IgG1 antibody. The proprietary peptide binds to all types of amyloid and delivers the antibody to the site of disease to stimulate the immune system to remove amyloid. The same PAR-peptide technology is utilized in AT-01.

About AT-03 PAR Therapeutic

AT-03 is a fusion of the company’s PAR-SAP (Serum Amyloid Protein) technology with a single-chain IgG1 Fc. The PAR-SAP component mediates binding to all types of amyloid deposits, and the single-chain Fc stimulates the immune system to remove amyloid deposits.

About AT-04 PAR Therapeutic

AT-04 is a fusion of our PAR-peptide technology with the Fc component of an IgG1 antibody. The PAR-peptide mediates binding to all types of amyloid and the Fc stimulates the immune system to remove amyloid. The same PAR-peptide technology is utilized in AT-01.

About Attralus  

Attralus is a clinical stage biopharmaceutical company focused on creating transformative medicines to improve the lives of patients with systemic amyloidosis. The company’s proprietary pan-amyloid removal (PAR) therapeutics are designed to directly bind to and remove toxic amyloid in organs and tissues. By targeting the universal disease-causing pathology in systemic amyloidosis diseases, PAR therapeutics have the potential to treat and reverse disease in patients with all types and stages of systemic amyloidosis. Attralus was founded by scientific experts in the field of amyloidosis and the company is headquartered in San Francisco. 

Forward-Looking Statements 

This press release contains forward-looking statements, including statements related to the efficacy, continued development, and potential of the Company’s product candidates. Words such as “novel,” “developing,” “first and only,” “potential,” “shown” and similar expressions are intended to identify forward-looking statements. These forward-looking statements are based upon Attralus' current expectations. Forward-looking statements involve risks and uncertainties. Attralus' actual results and the timing of events could differ materially from those anticipated in such forward-looking statements as a result of these risks and uncertainties. Attralus expressly disclaims any obligation or undertaking to release publicly any updates or revisions to any forward-looking statements contained herein to reflect any change in Attralus' expectations with regard thereto or any change in events, conditions, or circumstances on which any such statements are based.

Contact:

Luke Heagle
Real Chemistry
(910) 619-5764
lheagle@realchemistry.com


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