Peptide
                                                                                             sfAFP figure2                             

Polyproline II Helices in Biomolecular Condensates and amyloid formation
 

Challenge: Neurodegeneration

CSIC White books: Structural bases of life and evolution of macromolecular complexity (Challenge 2; CSIC white book vol.2)

PI: Douglas V. Laurents
     

Polyproline II helices play many essential roles in biomolecular condensates like nuclear speckles and the nucleolus, but their structure and stability are not fully understood.  Whereas protein design has made enormous strides in the last decade, novel structures are based exclusively on alpha helices and beta strands.  In this research line, we aim to use NMR spectroscopy and computational methods to improve our comprehension of polyproline II helices’ conformational, energetics and roles in membraneless organelles, and apply this knowledge to develop novel structures and biotech tools.

sfAFP figure1

In the image, Structure of the "snow flea" antifreeze protien dimer.

Publications

  • Treviño MÁ, Pantoja-Uceda D, Menéndez M, Gomez MV, Mompeán M, Laurents DV. The Singular NMR Fingerprint of a Polyproline II Helical Bundle. J Am Chem Soc. 2018;140(49):16988–17000. doi:10.1021/jacs.8b05261

Collaborators


Financing

  • Spanish MINECO grant: SAF2016-76678-C2-2-R; a new grant application to better characterize and develop designed structures, catalysts and biotech tools based on polyproline II helical bundles is currently under review.