Peptides based on the interface of hnRNPA2B1-transthyretin complex repress retinal angiogenesis in diabetic retinopathy.

ABSTRACT:

Background

Heterogeneous nuclear ribonucleoprotein A2B1 (hnRNPA2B1) plays a vital role in angiogenesis, when its nucleic acid-binding domain is occupied by transthyretin (TTR), the neovascularization of human retinal microvascular endothelial cells (hRECs) is repressed under hyperglycemic conditions.

Methods

HnRNPA2B1-targeting peptides (THIPs) were designed based on the core fragments at the TTR-hnRNPA2B1 interface. Biacore, Langmuir equilibrium adsorption, and co-immunoprecipitation (co-IP) assays were performed to determine the association between the THIPs and hnRNPA2B1. Proliferation and DNA synthesis in hRECs were detected using CCK-8 and EdU assays. Transwell, wound healing, and tube formation assays were used to evaluate migratory and the angiogenic capacity of hRECs

SUBMITTER: Chen Y 

PROVIDER: S-EPMC12008863 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature