Vittorio Bellotti is a medically qualified scientist who has worked on protein misfolding disorders both in the UK and Italy for over 20 years. His seminal demonstration that the amyloidogenic variants of lysozyme, discovered in the laboratory of Professor Sir Mark B. Pepys at the Royal Postgraduate Medical School, Hammersmith Hospital in 1993, were less stable than the wild type molecule provided the basis for a now generally accepted theory explaining the mechanism of amyloid conversion of globular proteins.

In 1995 he established an independent group at the University of Pavia carrying out pioneering work on β2-microglobulin fibrillogenesis causing dialysis-related amyloidosis. He made a series of key discoveries including the characterization of the pathogenic role of the truncated form of β2-microglobulin, ΔN6β2-microglobulin, ubiquitous in osteoarticular amyloid deposits, the demonstration that collagen and heparin could have a prominent role in amyloid fibril formation in vivo and the identification of a range of inhibitors of β2-microglobulin fibrillogenesis including nanobodies and doxycycline. He has also continued his association with the Pepys laboratory and was central to the identification of the transthyretin superstabiliser, mds84, and the subsequent collaboration with GlaxoSmithKline to develop this material as a potential transthyretin amyloidosis therapy.

He joined UCL in October 2011 with MRC Strategic Award, where he established a new group in the Centre for Amyloidosis and Acute Phase Proteins. At UCL he has continued his research into the molecular mechanisms of amyloidogenesis as exemplified in two recent studies, which both arose out of his work following the identification of new pathogenic variants of amyloidogenic proteins.
He identified the biochemical mechanisms underlying the pathogenicity of the first (and only) amyloidogenic variant of β2-microglobulin, D76N. This led to the seminal observation that forces generated under physiological conditions by agitation of fluids in the presence of hydrophobic-hydrophilic interfaces are sufficient to cause protein fibrillogenesis, and may represent a common mechanism of amyloidogenesis by globular proteins in vivo.
He identified a previously unrecognized step in the development of transthyretin amyloidosis by demonstrating that stress-mediated proteolysis is a pivotal step in the protein fibrillogenesis pathway.

His research strategy is inspired by the challenging objective of relating in vitro experimental conditions to the pathophysiological environment. He believes that the most efficient way to identify the underlying causes of complex diseases such as systemic amyloidosis is by collaboration between groups with complementary expertise and ideas. He has kept a close connection with his group in Pavia and continued to work with a network of longstanding collaborators in Italy including Professors Esposito (Udine), Relini (Genoa), Bolognesi (Milan), Cecconi (Modena).

At UCL he has developed a number of collaborations. These include work on alpha-synuclein (Professor Schapira), apolipoprotein C-III (Professor Talmud), structural insights into amyloidogenic proteins (Professor Christodoulou) and the generation of bio-compatible devices to study fibrillogenesis of human globular proteins (Professor Pinzani). Other external collaborations include the use of native mass spectrometry for protein structure analysis (Professor Robinson, Oxford) and work on new amyloidogenic variants of β2-microglobulin and apolipoprotein C-III (Professor Valleix, Paris).