BEGIN:VCALENDAR VERSION:2.0 PRODID:-//Ä¢¹½ÊÓÆµ//NONSGML v1.0//EN NAME:PhD defence A. Yeste Vázquez METHOD:PUBLISH BEGIN:VEVENT DTSTART:20250512T134500 DTEND:20250512T151500 DTSTAMP:20250512T134500 UID:2025/phd-defence-a-yeste-vazqu@8F96275E-9F55-4B3F-A143-836282E12573 CREATED:20250502T075256 LOCATION:(1st floor) Auditorium, Main building De Boelelaan 1105 1081 HV Amsterdam SUMMARY:PhD defence A. Yeste Vázquez X-ALT-DESC;FMTTYPE=text/html:
Constrained helical pep tides addressing intracellular targets
Peptides are naturally occurring biomolecules that are essential for many biological process es. In addition to their natural functions, they hold great potential as therapeutic agents because their size allows them to target surfa ces that are too large for small molecules, while still being more pe rmeable than larger biological drugs. However, their clinical applica tion is often limited by poor stability and low cell permeability.
Alejandro Yeste Vázquez investigated how chemical modifications can overcome these limitations and improve the pharmacological proper ties of peptides. He specifically focused on designing modified pepti des that can inhibit protein-protein interactions involved in the ons et and progression of diseases. With this work, Yeste Vázquez aims t o contribute to the development of new peptide-based therapies for di seases where traditional small molecules and biologics have proven in sufficient.
Yeste Vázquez demonstrates that it is possible to chemically tweak small protein-like molecules—known as peptides—t o make them more stable and enhance their ability to penetrate cells. However, he also emphasizes that there is no one-size-fits-all solut ion—how a peptide behaves depends heavily on its specific compositi on. While his research helps us understand how certain chemical chang es can improve these molecules, Yeste Vázquez also shows that each n ew peptide must be individually tested to determine what works best. This brings science one step closer to designing better, more effecti ve drugs based on these molecules.
More information on the thesis
DESCRIPTION: Peptides are naturally occurring biomolecules that are es sential for many biological processes. In addition to their natural f unctions, they hold great potential as therapeutic agents because the ir size allows them to target surfaces that are too large for small m olecules, while still being more permeable than larger biological dru gs. However, their clinical application is often limited by poor stab ility and low cell permeability. Alejandro Yeste Vázquez investigate d how chemical modifications can overcome these limitations and impro ve the pharmacological properties of peptides. He specifically focuse d on designing modified peptides that can inhibit protein-protein int eractions involved in the onset and progression of diseases. With thi s work, Yeste Vázquez aims to contribute to the development of new p eptide-based therapies for diseases where traditional small molecules and biologics have proven insufficient. Yeste Vázquez demonstrates that it is possible to chemically tweak small protein-like molecules� ��known as peptides—to make them more stable and enhance their abil ity to penetrate cells. However, he also emphasizes that there is no one-size-fits-all solution—how a peptide behaves depends heavily on its specific composition. While his research helps us understand how certain chemical changes can improve these molecules, Yeste Vázquez also shows that each new peptide must be individually tested to dete rmine what works best. This brings science one step closer to designi ng better, more effective drugs based on these molecules. More inform ation on the Constrained helical peptides addressing i ntracellular targets END:VEVENT END:VCALENDAR