Issue 9, 2018

Supramolecular propensity of suckerin proteins is driven by β-sheets and aromatic interactions as revealed by solution NMR

Abstract

Suckerin proteins are a family of block co-polymer-like structural proteins that self-assemble into robust supramolecular structures – the sucker ring teeth (SRT) – which are located on the arms and tentacles of cephalopods and used to firmly capture preys. Suckerins are promising biomimetic protein-based biopolymers, but the supramolecular interactions stabilizing SRT remain unknown. Here, we report multi-dimensional Nuclear Magnetic Resonance (NMR) spectroscopy structural studies of an engineered suckerin protein composed of two main sequence modules. The protein adopts a dynamic structure with regions in both module 1 (M1: residues A42–A52) and module 2 (M2: residues G30–Y37 and G58–Y65) folding into anti-parallel β-sheets and displaying β-strand propensity, respectively. The obtained structure highlights that aromatic residues present in glycine (Gly)-rich M2 modules are involved in π–π stacking interactions, leading to the stabilization of the structural core. In addition, hydrogen/deuterium (H/D) exchange studies demonstrate a high protection of residues involved in intra-molecular β-sheets. Gaining a better understanding of the molecular structure of suckerin provides key molecular lessons that may be mimicked in the de novo design of peptide- and protein-based biomaterials with applications in medicine, tissue engineering and nanotechnology.

Graphical abstract: Supramolecular propensity of suckerin proteins is driven by β-sheets and aromatic interactions as revealed by solution NMR

Supplementary files

Article information

Article type
Paper
Submitted
19 May 2018
Accepted
10 Jul 2018
First published
16 Jul 2018

Biomater. Sci., 2018,6, 2440-2447

Supramolecular propensity of suckerin proteins is driven by β-sheets and aromatic interactions as revealed by solution NMR

A. Kumar, H. Mohanram, K. W. Kong, R. Goh, S. Hoon, J. Lescar and A. Miserez, Biomater. Sci., 2018, 6, 2440 DOI: 10.1039/C8BM00556G

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements