Telomeres are nucleoprotein structures at the ends of human chromosomes that function to maintain genome stability. The unlimited proliferative capacity of cancer cells is dependent on their acquisition of a telomere maintenance mechanism to counteract the gradual telomere attrition that accompanies cellular proliferation. Alternative Lengthening of Telomeres (ALT) is a homologous recombination (HR)–mediated telomere maintenance mechanism utilised by approximately 15% of cancers in which ALT status often predicts poor prognosis. We have demonstrated that ZNF827 is recruited specifically to ALT telomeres, where it plays a multifaceted role in promoting ALT activity in concert with the nucleosome remodelling and deacetylase (NuRD) complex. Depletion of ZNF827 results in acute loss of ALT cell viability. To date, there are no other known functions of ZNF827, which makes it a novel potential target for ALT inhibition in cancers. Here we investigate the normal functions of ZNF827, and the mechanistic details of its recruitment and binding to ALT telomeres. We show that ZNF827 directly interacts with telomeric DNA displaying preferential binding to single stranded DNA. ZNF827 colocalises with DNA damage and repair proteins, indicative of a role for ZNF827 in DNA damage and HR-mediated repair. We propose that ZNF827 is a novel molecular target for ALT cancers, and aim to delineate the molecular interactions involved in the DNA damage response at ALT telomeres. Finally, we aim to explore potential synergistic effects of ZNF827 inhibition and DNA damage-inducing anticancer drugs such as topoisomerase inhibitors and PARP inhibitors for improved cancer therapeutics.