ASEA UNINET 2023/UniWien/02
| grant holder | Christian Schröder / K. Choowongkomon |
| funding period | 10/2023 - 09/2024 |
Abstract
The epidermal growth factor receptor (EGFR) is a transmembrane protein found on the surface of cells. It plays a crucial role in cell signaling pathways that control cell growth and division, as well as survival and differentiation. Dysregulation of EGFR signaling can lead to the development and progression of various cancers, including non-small cell lung cancer, head and neck cancer, and colorectal cancer.To better understand the role of EGFR in cancer, researchers have conducted extensive studies on the protein's structure, function, and genetic mutations that can lead to its activation. This research has led to the development of drugs targeting EGFR, such as tyrosine kinase inhibitors (TKIs) and monoclonal antibodies. These drugs effectively slow the growth of certain cancers and improve patient outcomes. Furthermore, research on EGFR has also been instrumental in developing personalized medicine. By analyzing an individual's genetic makeup, it is possible to determine if they carry mutations in the EGFR gene that may make them more susceptible to certain cancers. This information can help guide treatment decisions and improve patient outcomes. Cyclic peptides can serve as targeted inhibitors of EGFR signaling. EGFR is a transmembrane protein activated when it binds to specific growth factors, such as the epidermal growth factor (EGF). This binding initiates a cascade of signaling events that result in cell proliferation and survival. Cyclic peptides can act as antagonists of EGFR signaling by binding to the receptor and preventing it from interacting with its ligands, such as EGF. This binding can be highly specific and selective as the cyclic structure allows for better shape complementarity with the receptor resulting in more specific and stronger interactions, making cyclic peptides attractive candidates for targeted therapy. Additionally, cyclic peptides are more resistant to proteolytic degradation than linear peptides, making them more stable in vivo and, thus, more appealing for pharmacokinetics and bioavailability.
