Controlling the Oligomerization State of Aβ-Derived Peptides with Light.

ABSTRACT: A key challenge in studying the biological and biophysical properties of amyloid-forming peptides is that they assemble to form heterogeneous mixtures of soluble oligomers and insoluble fibrils. Photolabile protecting groups have emerged as tools to control the properties of biomolecules with light. Blocking intermolecular hydrogen bonds that stabilize amyloid oligomers provides a general strategy to control the biological and biophysical properties of amyloid-forming peptides. In this paper we describe the design, synthesis, and characterization of macrocyclic β-hairpin peptides that are derived from amyloidogenic peptides and contain the N-2-nitrobenzyl photolabile protecting group. Each peptide contains two heptapeptide segments from Aβ_16-36 or Aβ_17-36 constrained

SUBMITTER: Salveson PJ 

PROVIDER: S-EPMC6361387 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature