In 1989, Andrea Brancaccio received a degree in Biology at the University of Rome La Sapienza, in the Department of Biochemistry, under the supervision of Prof. Maurizio Brunori. He studied the cross-linking of hemoglobin with a diaspirinic compound which increases its thermostability. Afterwards, he started his graduate training. At the beginning, he studied the effect of increasing amounts of sucrose on the allosteric behaviour of hemoglobin. His research interests afterwards focused on the structural-functional relationships in recombinant myoglobins. He investigated the role of several mutations in the active site (Brancaccio et al., Journal of Biological Chemistry, 1994). He obtained his PhD degree in Biochemistry in 1994.

He then moved to the Biozentrum of the University of Basel with a post-doctoral position in the laboratory of Prof. Jürgen Engel where his research interest focused on the extracellular matrix and in particular on dystroglycan. During this period, he collected the very first structural data on α-dystroglycan using electron microscopy on the native molecule as well as on some recombinant fragments, thus discovering an N-terminal autonomous module whose structure he subsequently contributed to solve by X-ray crystallography (Bozic et al., Journal of Biological Chemistry, 2004). During his post-doc he also investigated structurally and functionally the interaction between agrin and α-dystroglycan. In 1998 he moved back to Italy to join CNR at the Institute of Chemistry of Molecular Recognition (now Institute of Chemical Sciences and Technologies), where his main research interest is still the structural-functional relationships of dystroglycan.

Over the last 10 years, he has spent long periods as a visiting scientist at the School of Biochemistry of the University of Bristol (UK), where he was initially involved on a project on Archaeal chaperonins while he kept following his main interest in dystroglycan and other extracellular matrix proteins. During these years, he was senior author of a series of structural papers on the N-terminal domain of α-dystroglycan (WT and mutated) which underlined the importance of its highly flexible structure in the intracellular maturation of the dystroglycan precursor. Following on this line of work, the recently characterized and ever-growing group of primary dystroglycanopathies became central to its research focus. In parallel with this experimental work, he has performed bioinformatic analyses investigating a series of evolutionary aspects of the dystroglycan protein and gene (Adams & Brancaccio, Biology Open, 2015) and of the enzymes responsible for its post-translational modification (Bigotti & Brancaccio, Open Biology, 2021).

His work on the transmembrane β-subunit of dystroglycan recently resulted in the characterization of a site-directed mutant of its ectodomain, C667F. This mutation was shown to cause a severe Muscle-Eye-Brain disease phenotype, and using a combined approach based on cellular biochemistry and super-resolution microscopy, Dr. Brancaccio and collaborators demonstrated that the mutated polypeptide is engulfed in the ER/Golgi (Signorino et al., Human Mutation, 2018). The murine knockin model of this mutation has been established and is under analysis in collaboration with the University of Bonn. He has been the recipient of a bilateral CNR-CINVESTAV grant (2019-2020) for analyzing the interactors of β-dystroglycan in the nucleus and has meanwhile started a new project (funded 2024-2026) within the Medical School of Bristol University on the potential involvement of the agrin-dystroglycan axis in cardiomyocytes regeneration (Bigotti et al., Front Bioeng Biotechnol., 2020). Currently, in Bristol he is also investigating the anti-viral properties of the α-dystroglycan N-terminus (with 2 grants and 1 patent awarded so far to this project).