Siermann, Paulien Alida Hendrica (2025) Computational design of high-affinity protein binders targeting the HSV-1 viral protein UL12.5. Bachelor's Research Project, Pharmacy.
|
Text
bPHAR2025SiermannPAH.pdf Download (1MB) | Preview |
|
![[img]](https://fse.studenttheses.ub.rug.nl/style/images/fileicons/text.png) |
Text
Toestemming.pdf Restricted to Registered users only Download (190kB) |
Abstract
Herpes simplex virus type 1 (HSV-1) is a highly prevalent pathogen. While most infections are either asymptomatic or cause oral sores, the virus poses serious health risks, particularly for immunocompromised individuals. Current treatment strategies are ineffective against HSV-1 in its latent state, allowing for viral reactivation and recurrence. The HSV-1 viral UL12.5 protein plays a key role in mitochondrial DNA (mtDNA) degradation and contributes to viral reactivation. This research project focuses on designing de novo protein binders that target UL12.5, with the goal of developing a novel therapeutic strategy to prevent HSV-1 reactivation and recurrence. Using a computational approach 1500 proteins binders against UL12.5 were designed. Unfortunately, none of the designed binders were identified to be high-affinity binders, and are therefore unlikely to prevent UL12.5 from degrading mtDNA or prevent the recurrence of active infection. Future studies could improve by targeting the designed binders towards specific binding spots essential for UL12.5’s activity. Once these binders are shown to bind to UL12.5 with high-affinity, their ability to prevent mtDNA degradation and recurrence can be evaluated through in vitro and in cellulo experiments, contributing to the development of novel therapeutics against HSV-1.
| Item Type: | Thesis (Bachelor's Research Project) |
|---|---|
| Supervisor name: | Rafie, K. |
| Degree programme: | Pharmacy |
| Thesis type: | Bachelor's Research Project |
| Language: | English |
| Date Deposited: | 08 Apr 2025 06:53 |
| Last Modified: | 08 Apr 2025 06:53 |
| URI: | https://fse.studenttheses.ub.rug.nl/id/eprint/34995 |
Actions (login required)
 |
View Item |