Fibrillins are large family of proteins that form a major constituent of
microfibrils and subsequently the extracellular matrix. Fibrillin-1 is the most
characterized fibrillin member and has been verified to be linked to Marfan
syndrome. Fibrillin-2 was linked to congenital contractural arachnodactyly.
Fibrillin-3 is expressed during tissues development and it has been linked to
Weill Marchesani syndrome and polycystic ovary syndrome. Self-assembly
and multiple ligand binding properties of fibrillins are crucial for the proper
formation and function of microfibrils. These properties are often
compromised in pathological situations. Therefore, we aimed to study the
interaction epitopes of the N-terminal of fibrillin-3 with fibulin-2 and heparin
in comparison to fibrillin-1, as well as the molecular shapes of the Nterminal region of fibrillin-3. In the present study we compared the binding
of fibulin-2 and heparin to the N-terminal polypeptides of both fibrilin-1 and
fibrillin-3. Also, we compared folding shapes of their N-termini. Our results
indicated the similarity of N-termini of both fibrillin-1 and fibrillin-3 in
binding to fibulin-2 and heparin as well as their structures. The N-terminal
polypeptides of Fibrillin-3 can interact with Fibulin-2 and heparin in a
similar fashion as compared to fibrillin-1, indicating similar functions for
both isoforms.
