Seagull Therapeutics
Reprogramming
the Tumor Micro-Environment
About Seagull
SeaGull Therapeutics is focused on reprogramming the Tumor Micro Environment for more effective treatment of solid tumors. SeaGull’s lead project, SGL10060, is a fusion protein based on innovative science from the University of Turin.
Meet our teamReprogramming the tumor micro environment TME
The TME is where the tumor modifies local structures and cells to protect itself from the body’s own immune system and from therapeutic strategies. By reprograming the TME, we help the body fight the tumor and enhance anti-cancer therapies for improved patient outcomes.
Read our publicationsOur protein candidate SGL10060
SGL10060 is fusion protein based on Semaphorin3A and selectively targeting PlexinA4. This protein possesses the anti-tumoral proprieties of Semaphorin3A without the known pro-tumoral traits.
Read More Ashley is a chemist with an MBA and has spent his career on the business side of science. He has
worked with small and large companies, managing contacts and alliances and growing businesses. At
Domain Therapeutics, Ashley has identified and closed product and technology deals, and helped to
create spin off companies in line with company strategy.
Ashley Nagle
SeaGull Therapeutics CEO/Chairman,
Domain Strategic & Business Director
Stephan has a PhD in Medicinal Chemistry from University of Strasbourg, France. Since 2008,
Stephan has led R&D at Domain Therapeutics for both its internal and externalized pipeline. He was
involved in the identification of Foliglurax, currently in Phase II development for Parkinson’s disease.
Stephan Schann
SeaGull Therapeutics R&D Advisor,
Domain R&D Director
Pascal holds a PhD in molecular biology from the University of Strasbourg. He was appointed
Assistant Professor at the University of Geneva before joining Transgene SA as an R&D project
leader. Soon after its creation, he joined Faust Pharmaceuticals SA as CSO. He founded Domain in
2008 and has been CEO / CSO since.
Pascal Neuville
SeaGull Therapeutics Board,
Domain CEO/CSO
Guido Serini MD, Ph.D
Professor of Clinical Biochemistry and Molecular Biology, University of Turin
More Guido heads the Laboratory of Cell Adhesion Dynamics of the Candiolo Cancer Institute in Turin, Italy.
Over the last 20 years, he studied the role of integrin-mediated cell adhesion in blood vessel
formation. He has shown that SEMA3A can be therapeutically reintroduced to inhibit tumor growth
and extend survival.
Guido Serini MD, Ph.D
Professor of Clinical Biochemistry and Molecular Biology, University of Turin
Close Enrico leads the Transgenic Mouse Models laboratory at the Candiolo Cancer Institute in Turin. Over
the last 20 years he has investigated the role of the tumor microenvironment in regulating
metastatic growth. He has shown that Sema3A is able to overcome resistance to anti-angiogenic
therapies, by normalizing tumor vessels and reducing hypoxia.
Enrico Giraudo Ph.D
Professor of Biochemistry at the Faculty of Pharmacy, University of Turin
CloseLuca Tamagnone MD, Ph.D
Professor of Histology at the School of Medicine, Sacred Heart University of Rome
More Luca was nominated EMBO Young Investigator in 2001, and from 2003 to 2018 led a renowned research laboratory in Cancer Cell Biology at the Candiolo Cancer Institute. He has been at the forefront of research on Semaphorins, identifying fundamental signalling mechanisms and functional activities in normal and cancer cells.
Luca Tamagnone MD, Ph.D
Professor of Histology at the School of Medicine, Sacred Heart University of Rome
CloseAbout SGL10060
SGL10060 is a fusion protein based on Semaphorin3A that strongly inhibits solid tumors. The key features of SGL10060 are:
- Normalization of the tumor vasculature and reduction of hypoxia
- Change of the immune cell population within the tumor
- Reduction of metastasis
- Combination with a wide range of SOC therapies
Tumor vasculature normalization
Tumors possess a poorly functional vasculature, causing formation of hypoxic regions that trigger an escape program in tumor cells and eventually lead to metastatic dissemination. SGL10060 acts on tumor vasculature, promoting maturation of blood vessels, strongly reducing hypoxia and the drivers for tumor cells to escape.
The resulting normalization of the vasculature also allows therapeutic molecules and immune cells better access to the tumor.
Immune cell population
Progressing tumors contain pro-tumoral macrophages that suppress anti-tumor immunity by preventing activation of dendritic cells, cytotoxic T-lymphocytes (CD8+) and natural killer cells. SGL10060 triggers a switch in the macrophage population by promoting anti-tumoral macrophage proliferation.
These macrophages are characterized by pro-inflammatory activity and antigen presentation allowing proper CD8+ activation for an efficient anti-tumor response.
Metastasis
Through reprogramming the TME, normalizing the blood vessels, reducing hypoxia and changing the immune cell population, metastasis of the tumor is greatly inhibited.
This is because the drivers for the tumor to escape from its environment have been reduced, and the escape route through leaky blood vessels removed.
Combination therapies
Studies have shown that SGL10060 can be combined with existing chemotherapeutic drugs to increase their efficacy in the treatment of solid tumors.
Given the effect of SGL10060 on immune cells, additional combinations with immune-oncology treatments are being explored. Preliminary studies have shown an improved efficacy of these therapies when combined with SGL10060.
News & Publications
SeaGull attending BioEquity
05/01/2019#Event
SeaGull will be at BioEquity in Barcelona for discussions with investors and partners.
If you would like to know more about the company, our lead product SGL10060 and our plans, please contact us through the partnering system and we can arrange to meet.
A rationally designed NRP1-independent superagonist SEMA3A mutant is an effective anticancer agent
05/23/2018#Publication
Gioelli N, …, Tamagnone L, Giraudo E, Serini G
A rationally designed, safe, parenterally deliverable, NRP1-independent SEMA3A mutant fusion protein that binds PLXNA4 with nanomolar affinity and has much greater biochemical and biological activities that SEMA3A. In vivo, the fusion protein successfully normalized the vasculature, inhibited tumor growth, curbed metastatic dissemination, and effectively improved the supply and anticancer activity of chemotherapy.
Class 3 semaphorins: physiological vascular normalizing agents for anti-cancer therapy
02/15/2013#Publication
Serini G, Bussolino F, Maione F & Giraudo E
Findings from preclinical and clinical studies show that vascular normalization represents a novel strategy to enhance the efficacy of and overcome the acquired resistance to anti-angiogenic therapies in cancer. Class 3 semaphorins, which regulate axon guidance and angiogenesis, have been identified as vascular normalizing agents that inhibit metastatic dissemination by restoring vascular function and impacting different cellular components of the tumour microenvironment.
Semaphorin 3A overcomes cancer hypoxia and metastatic dissemination induced by antiangiogenic treatment in mice
04/09/2012#Publication
Maione F, Capano S, …, Bussolino F, Serini G and Giraudo E
Semaphorin 3A (Sema3A) expression overcomes the proinvasive and prometastatic resistance observed upon angiogenesis reduction by sunitinib in both pancreatic neuroendocrine tumors (PNETs) and cervical carcinomas. By improving cancer tissue oxygenation and extending the normalization window, Sema3A counteracted sunitinib-induced activation of hypoxia-dependent signaling pathways and reduced tumor hypoxia.