Ameloblastin binding to biomimetic models of cell membranes - A continuum of intrinsic disorder.

ABSTRACT:

Objective

A 37-residue amino acid sequence corresponding to the segment encoded by exon-5 of murine ameloblastin (Ambn), AB2 (Y67-Q103), has been implicated with membrane association, ameloblastin self-assembly, and amelogenin-binding. Our aim was to characterize, at the residue level, the structural behavior of AB2 bound to chemical mimics of biological membranes using NMR spectroscopy.

Design

To better define the structure of AB2 using NMR-based methods, recombinant ¹³C- and ¹⁵N-labelled AB2 (*AB2) was prepared and data collected free in solution and with deuterated dodecylphosphocholine (dPC) micelles, deuterated bicelles, and both small and large unilamellar vesicles.

Results

Amide chemical shift and intensity perturbations observed in ¹

SUBMITTER: Buchko GW 

PROVIDER: S-EPMC12165007 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature