Every second, billions of molecules inside our bodies recognize one another, assemble into structures, transport cargo, send signals, or defend us from infection. Much of this invisible activity depends on proteins: sophisticated molecular machines built from simple building blocks called amino acids.
Peptides are short chains of amino acids and can be considered simplified versions of proteins. Yet despite their smaller size, they retain many of the properties that make proteins so remarkable. They can selectively recognize other molecules and, under the right conditions, spontaneously organize into larger and more complex structures. This combination of molecular recognition and self-assembly is what makes peptides such versatile tools for modern science, and researchers are now learning how to exploit these design principles to develop new medicines and adaptive materials, among many other applications.
One particularly interesting area is cancer therapy. Chemotherapy-resistant tumors remain one of the greatest challenges in oncology because cancer cells can evolve mechanisms that allow them to survive treatment and eventually relapse. Unlike many conventional drugs, peptides can often be engineered with extraordinary precision. Small changes in their amino acid sequence can dramatically alter their stability, structure, or the biological targets they recognize.
At CICA, we are exploring whether peptides can selectively target resistant ovarian cancer cells while sparing healthy tissues. Our approach focuses on designing peptides capable of recognizing proteins that are elevated in resistant tumor cells. So far, we have identified a family of peptides that inhibits the activity of one of these proteins and selectively induces the death of resistant ovarian cancer cells in vitro while showing minimal effects on non-tumoral cells.
But peptides are interesting not only as drugs. Certain peptide sequences can also self-assemble into fibers and nanostructures thousands of times smaller than the width of a human hair. Inspired by the dynamic behavior of biological systems, we are developing peptide-based nanostructures capable of responding to external stimuli such as changes in pH. In some of our designs, self-assembly is based on coiled coil motifs: helical peptide structures that selectively recognize and organize with one another. Under specific conditions, our assemblies form fibrillar nanostructures that can later disassemble in response to external stimuli. Remarkably, this dynamic behavior can directly influence how cells interact with materials.
When incorporated into biomaterial scaffolds, these peptide fibers mimic aspects of the natural extracellular matrix surrounding cells in tissues. By triggering fiber disassembly through chemical stimuli, we can modulate cell adhesion to the scaffold surface. In other words, changing molecular organization at the nanoscale translates into a macroscopic biological response. Such materials could eventually find applications in tissue engineering, regenerative medicine, or smart biomedical devices capable of dynamically interacting with living cells.
We believe peptide research is particularly fascinating because it sits at the intersection of chemistry, biology, materials science, and medicine. Peptides are not only potential therapeutics or biomaterials, but they also provide a way of understanding how nature builds complex functions from relatively simple molecular instructions and how these same rules can inspire entirely new technologies.
Elena Pazos is an Oportunius Research Professor at the CICA - Centro Interdisciplinar de Química e Bioloxía and the Department of Chemistry at the Universidade da Coruña (UDC). Her research lies at the interface of chemical biology, supramolecular chemistry, and peptide engineering, with a focus on designing functional molecular systems capable of molecular recognition and controlled self-assembly.
She obtained her PhD under the supervision of Prof. José L. Mascareñas and Prof. M. Eugenio Vázquez at the Universidade de Santiago de Compostela, working on luminescent sensors for cancer-related proteins. During her doctoral studies, she carried out research stays at Trinity College Dublin (with Prof. Thorfinnur Gunnlaugsson) and the University of Illinois at Urbana–Champaign (with Prof. Scott Silverman).
In 2012 she received a Fundación Barrié postdoctoral fellowship to join Prof. Samuel I. Stupp at Northwestern University, where she worked on supramolecular peptide nanostructures for biomedical applications. She later held research positions in both industry and academia, including work with Prof. Ramón A. Álvarez-Puebla at the Centre Tecnològic de la Química de Catalunya as a TECNIOspring / Marie Skłodowska-Curie researcher, before joining CICA in 2017 through the InTalent UDC–Inditex Programme.
Her work has been recognized with several competitive distinctions, including an ERC Starting Grant (2019), a Ramón y Cajal contract (2020), and an ERC Proof of Concept grant (2025).