Ana Salome Veiga
Assistant Professor
Gulbenkian Institute for Molecular Medicine
Talk Information
Exploration of Selectivity and Methods for Targeting Disease
18 June 2025, 05:00pm - 05:15pm, in the Pacific Jewel Ballroom
L50 – Unveiling the Mode of Aaction of SARS-CoV-2 Putative Fusion Peptides and their Exploitation as Antiviral Targets
Dr. Ana Salomé Veiga is an Assistant Professor at the Gulbenkian Institute for Molecular Medicine, GIMM, in Lisbon, Portugal. Her research focuses on the design and characterization of antiviral and antimicrobial peptides, with particular emphasis on their mechanisms of action and potential therapeutic applications.
Academic Background
Dr. Veiga earned her Ph.D. in Biochemistry from the University of Lisbon. She has since established herself as a leading researcher in the field of peptide-based therapeutics, contributing significantly to our understanding of peptide interactions with biological membranes and their role in combating infectious diseases.
Research Focus
At GIMM, Dr. Veiga leads a research group dedicated to exploring the biophysical and biochemical properties of peptides derived from viral proteins. Her work aims to develop novel therapeutic agents capable of targeting viral infections and overcoming challenges such as drug resistance and delivery across biological barriers.
Notable Contributions
Dr. Veiga has made significant contributions to the field of peptide therapeutics, including the development of proteolysis-resistant peptides with potent anti-HIV-1 activity. Her research has been published in high-impact journals and has advanced our understanding of peptide-based interventions against viral pathogens.
Professional Engagements
Dr. Veiga is actively involved in the scientific community, serving as a reviewer for several peer-reviewed journals and participating in international conferences. She is also committed to mentoring the next generation of scientists, supervising graduate students and postdoctoral researchers in her laboratory.
Through her innovative research and dedication to scientific advancement, Dr. Ana Salomé Veiga continues to contribute to the development of effective peptide-based therapies for infectious diseases.
Unveiling the Mode of Action of SARS-CoV-2 Putative Fusion Peptides and Their Exploitation as Antiviral Targets
1 Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal
2 Faculdade de Medicina, Universidade de Lisboa, Lisboa, Portugal
3 Gulbenkian Institute for Molecular Medicine, Lisboa, Portugal
4 Centro de Engenharia Biológica, Escola de Engenharia da Universidade do Minho, Braga, Portugal
5 Cell Biology of Viral Infection Lab, Católica Biomedical Research Centre, Oeiras, Portugal
SARS-CoV-2 entry into host cells is mediated by the spike glycoprotein (S-protein), through a process that results in the fusion of the host and viral membranes. The fusion peptide (FP) is a key domain of the S-protein, known to insert into and disturb the host membrane. Once the FP anchors the virus to the host cell, the S-protein undergoes conformational changes allowing the completion of fusion. Despite its crucial role in viral entry, the region within the S-protein that corresponds to the FP is not yet fully clear. To shed light on this matter, we combined computational and experimental methods to characterize two previously proposed putative FPs, the N-terminal FP (nFP) and the internal FP (iFP).
Our results indicate that the iFP has a stronger affinity for membranes and exhibits higher hydrophobicity compared to the nFP, which tends to localize at the membrane-water interface. Moreover, the iFP causes higher membrane perturbation than the nFP, inducing lipid mixing and lipid vesicle content leakage. Furthermore, engineered spike-pseudotyped lentiviruses containing substitutions on the iFP region are unable to infect cells. These findings suggest that the nFP may play a role in the initial interaction with the membrane, possibly facilitating the deeper insertion of the iFP and its role in promoting membrane fusion. The FP and other S-protein domains were used as targets to inhibit membrane fusion and block viral entry. Inhibitory small proteins were computationally designed resulting in a viral neutralization in the low micromolar range. Our study propose important insights to understand and inhibit the SARS-CoV-2 fusion machinery.