Conformational dynamics of human IAPP monomers

Ronan D. Murphy, Jennifer Conlon, Tayyaub Mansoor, Sorin Luca, Sara Vaiana, Nicolae Viorel Buchete

Research output: Contribution to journalArticlepeer-review

23 Scopus citations


We study the conformational dynamics of the human Islet Amyloid Polypeptide (hIAPP) molecule - a 37 residue-long peptide associated to type 2 diabetes - using molecular dynamics (MD) simulations. We identify partially structured conformational states of the hIAPP monomer, categorized by both end-to-end distance and secondary structure, as suggested by previous experimental and computational studies. The MD trajectories of hIAPP are analyzed using data-driven methods, in particular principal component analysis, in order to identify preferred conformational states of the amylin monomer and to discuss their relative stability as compared to corresponding states in the amylin dimer. These potential hIAPP conformational states could be further tested and described experimentally, or in conjunction with modern computational analysis tools such as Markov state-based methods for extracting kinetics and thermodynamics from atomistic MD trajectories.

Original languageEnglish (US)
Pages (from-to)1-7
Number of pages7
JournalBiophysical Chemistry
StatePublished - Jun 2012


  • Conformational analysis
  • Data-driven kinetic analysis
  • Human Islet Amyloid Polypeptide (hIAPP)
  • Molecular dynamics
  • Type 2 diabetes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Organic Chemistry


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