Afsaneh Sadre Momtaz

Afsaneh Sadre Momtaz
North Carolina Agricultural and Technical State University | NC A&T · Joint School of Nanoscience and Nanoengineering-Department of Nanoengineering

Doctor of Philosophy

About

6
Publications
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Introduction
Afsaneh Sadre Momtaz worked as a postdoc researcher at the Groningen Research Institute of Pharmacy (GRIP), University of Groningen, for two years. Afsaneh currently works as a postdoc researcher at Joint School of Nanoscience and Nano engineering, University of North Carolina.

Publications

Publications (6)
Article
Full-text available
The SARS-CoV-2 viral spike protein S receptor-binding domain (S-RBD) binds ACE2 on host cells to initiate molecular events, resulting in intracellular release of the viral genome. Therefore, antagonists of this interaction could allow a modality for therapeutic intervention. Peptides can inhibit the S-RBD:ACE2 interaction by interacting with the pr...
Conference Paper
Background Tumor growth depends on pro-angiogenic vascular endothelial growth factors (VEGF-A/-B) via binding to VEGF receptors (VEGFR1 and VEGFR2) that are biomarkers of tumor angiogenesis. Importantly, interfering with this interaction by small molecules impairs tumor growth and angiogenesis. Methods A novel peptide (known as VGB3) was synthesiz...
Article
Full-text available
Insert abstract text here. RGD peptides represent the most outstanding recognition motif involved in cell adhesion and binds to αvβ3 integrin that has been targeted for cancer therapy. Various RGD-containing peptides and peptidomimetics have been designed and synthesized to selectively inhibit this integrin. In this study, the synthesis of RGD base...
Article
Full-text available
ABSTRACT Background: Vascular endothelial growth factor (VEGF) A and B are endothelial cell mitogens whose ligation to VEGFR1/VEGFR2 drives tumor angiogenesis and metastasis, and epithelial-mesenchymal transition (EMT). Blockade of these signaling axes could be obtained by disturbing the interactions between VEGFA and/or VEGFB with VEGFR1 and/or VE...
Article
Background: Neutralization of vascular endothelial growth factor receptor 1 (VEGFR1) and/or VEGFR2 is a widely used means of inhibiting tumor angiogenesis. Methods: Based on the complex X-ray structures of VEGFA/VEGFR1, VEGFA/VEGFR2, and VEGFB/VEGFR1, a peptide (referred to as VGB) was designed to simultaneously bind to VEGFR1 and VEGFR2, and bindi...

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Projects

Projects (4)
Archived project
Cancer metastasis is responsible for a majority of the mortality in cancer patients and involves complex interactions, modulated by various factors and cytokines, between malignant and host cells. Vascular endothelial growth factor (VEGF) A and B are endothelial cell mitogens whose ligation to VEGFR1/VEGFR2 drives tumor angiogenesis and metastasis, and epithelial-mesenchymal transition (EMT). Blockade of these signaling axes could be obtained by disturbing the interactions between VEGFA and/or VEGFB with VEGFR1 and/or VEGFR2. Our project showed that VEGF-B produced by tumor cells significantly remodels tumor microvasculature, leading to leaky vascular networks that are highly permissive for tumor cell invasion. In this project, a de nevo designed peptide that recognizes both VEGFR1 and VEGFR2 were investigated for its inhibitory effects on the VEGF-induced angiogenesis. We investigated the inhibitory effects of peptide on downstream mediators of metastasis.
Archived project
Angiogenesis is critical to the growth of human tumors and the development of metastasis. Amongst the many proangiogenic mechanisms identified, the vascular endothelial growth factor (VEGF) signaling pathway has been implicated as the key regulator of tumor neovascularisation. Various therapeutic agents targeting the VEGF pathway have been successfully developed. The aim of this project was to develop a simplified system to enable the rational design of inhibitor of VEGFB–VEGFA/VEGFR1D2 system (PDB ID:2XAC and 1FLT). Among large surface areas comprising five main interacting regions, a small peptide antagonist could be designed and only act at a single site covering a small surface area with high-affinity interaction.
Project
We have discovered and patented a series (6) of highly novel high affinity binders of the CoV-2 S-RBD that inhibit the first steps in viral cell entry. These peptides have a high potential to provide a therapeutic treatment for COVID-19 patients by antagonizing the interaction of S-RBD with the ACE2 host cell receptor.