Probing the interplay between calcitonins and islet amyloid polypeptides with membranes using advanced fluorescence methodologies

22/03/2019

The conversion of peptides/proteins from their native soluble states into β-sheet-rich fibrillar assemblies is the hallmark of several human diseases. Biological membranes can modulate amyloid fibril formation in vivo, increasing its complexity. Here, calcitonin (CT) and islet amyloid polypeptide (IAPP) were used as model polypeptides to obtain a mechanistic understanding of how anionic lipid membranes influence their fibrillation pathways. Comparative biophysical studies of the selfassembly of the human amyloidogenic (hCT and hIAPP, respectively) and a control non-amyloidogenic variant of each peptide (salmon (sCT) and rat (rIAPP) sequences, respectively) were performed to elucidate the structural and dynamic features of the oligomeric intermediates formed in each case. Fluorescent conjugates of the peptides were used to increase the scope of the applied advanced fluorescence techniques.

Autores da comunidade :

• 

  J

  Joana Catarina Ribeiro Ricardo

  ist90628

Orientadores desta instituição:

• 

  A

  Ana Isabel Abrantes Coutinho

  ist90114

• 

  M

  Manuel José Estevez Prieto

  ist10881

101453795

Doutoramento em Química

chemical-sciences - Química

eng - Inglês

Instituto Superior Técnico