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

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...

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Main Authors: Kumar, Akshita, Mohanram, Harini, Kong, Kiat Whye, Goh, Rubayn, Hoon, Shawn, Lescar, Julien, Miserez, Ali
Other Authors: School of Materials Science and Engineering
Format: Article
Language:English
Published: 2020
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Online Access:https://hdl.handle.net/10356/140912
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-1409122020-06-03T01:42:01Z Supramolecular propensity of suckerin proteins is driven by β-sheets and aromatic interactions as revealed by solution NMR Kumar, Akshita Mohanram, Harini Kong, Kiat Whye Goh, Rubayn Hoon, Shawn Lescar, Julien Miserez, Ali School of Materials Science and Engineering School of Biological Sciences Center for Biomimetic Sensor Science NTU Institute of Structural Biology Engineering::Materials Supramolecular Propensity Suckerin Proteins 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. ASTAR (Agency for Sci., Tech. and Research, S’pore) MOE (Min. of Education, S’pore) 2020-06-03T01:42:00Z 2020-06-03T01:42:00Z 2018 Journal Article Kumar, A., Mohanram, H., Kong, K. W., Goh, R., Hoon, S., Lescar, J., & Miserez, A. (2018). Supramolecular propensity of suckerin proteins is driven by β-sheets and aromatic interactions as revealed by solution NMR. Biomaterials Science, 6(9), 2440-2447. doi:10.1039/c8bm00556g 2047-4830 https://hdl.handle.net/10356/140912 10.1039/c8bm00556g 30042992 2-s2.0-85052147771 9 6 2440 2447 en Biomaterials Science © 2018 The Royal Society of Chemistry. All rights reserved.
institution Nanyang Technological University
building NTU Library
country Singapore
collection DR-NTU
language English
topic Engineering::Materials
Supramolecular Propensity
Suckerin Proteins
spellingShingle Engineering::Materials
Supramolecular Propensity
Suckerin Proteins
Kumar, Akshita
Mohanram, Harini
Kong, Kiat Whye
Goh, Rubayn
Hoon, Shawn
Lescar, Julien
Miserez, Ali
Supramolecular propensity of suckerin proteins is driven by β-sheets and aromatic interactions as revealed by solution NMR
description 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.
author2 School of Materials Science and Engineering
author_facet School of Materials Science and Engineering
Kumar, Akshita
Mohanram, Harini
Kong, Kiat Whye
Goh, Rubayn
Hoon, Shawn
Lescar, Julien
Miserez, Ali
format Article
author Kumar, Akshita
Mohanram, Harini
Kong, Kiat Whye
Goh, Rubayn
Hoon, Shawn
Lescar, Julien
Miserez, Ali
author_sort Kumar, Akshita
title Supramolecular propensity of suckerin proteins is driven by β-sheets and aromatic interactions as revealed by solution NMR
title_short Supramolecular propensity of suckerin proteins is driven by β-sheets and aromatic interactions as revealed by solution NMR
title_full Supramolecular propensity of suckerin proteins is driven by β-sheets and aromatic interactions as revealed by solution NMR
title_fullStr Supramolecular propensity of suckerin proteins is driven by β-sheets and aromatic interactions as revealed by solution NMR
title_full_unstemmed Supramolecular propensity of suckerin proteins is driven by β-sheets and aromatic interactions as revealed by solution NMR
title_sort supramolecular propensity of suckerin proteins is driven by β-sheets and aromatic interactions as revealed by solution nmr
publishDate 2020
url https://hdl.handle.net/10356/140912
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