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Structural Proteins from Whelk Egg Capsule with Long Range Elasticity Associated with a Solid-State Phase Transition

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‡ Biomolecular Sciences and Engineering Program, University of California, Santa Barbara, California 93106, United States
§ School of Materials Science and Engineering, Nanyang Technological University, Singapore 639798
∥ Center for Biomimetic Sensor Science, Nanyang Technological University, Singapore 637553
⊥ Austrian Institute of Technology GmbH, AIT, Donau-City Str. 1, 1220 Vienna, Austria
# School of Biological Sciences, Nanyang Technological University, Singapore 637551
*E-mail: [email protected]; [email protected]
Cite this: Biomacromolecules 2014, 15, 1, 30–42
Publication Date (Web):December 18, 2013
https://doi.org/10.1021/bm401598z
Copyright © 2013 American Chemical Society
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    Abstract

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    The robust, proteinaceous egg capsules of marine prosobranch gastropods (genus Busycotypus) exhibit unique biomechanical properties such as high elastic strain recovery and elastic energy dissipation capability. Capsule material possesses long-range extensibility that is fully recoverable and is the result of a secondary structure phase transition from α-helical coiled-coil to extended β-sheet rather than of entropic (rubber) elasticity. We report here the characterization of the precursor proteins that make up this material. Three different proteins have been purified and analyzed, and complete protein sequences deduced from messenger ribonucleic acid (mRNA) transcripts. Circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy indicate that the proteins are strongly α-helical in solution and primary sequence analysis suggests that these proteins have a propensity to form coiled-coils. This is in agreement with previous wide-angle X-ray scattering (WAXS) and solid-state Raman spectroscopic analysis of mature egg capsules.

    Supporting Information

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    Table S1: N-termini Edman sequencing results of Bc-CPs from individual SDS-PAGE bands of crude extract. Figure S1: 1% agarose gel of RT-PCR with 3′ RACE products. Figure S2: Complete amino acid sequences of (a) CP-1b and (b) CP-2, as deduced from cDNA. Figure S3: CD spectra of mixtures of CP-1 and CP-2 in various ratios. Figure S4: ATR-FTIR spectra of CP-1 and CP-3, showing the preferential formation of β-sheets over α-helices when the proteins are freeze-dried from concentrated, compared to diluted, solutions. Figure S5: (a) ATR-FTIR spectra of egg case, showing a loss of Amide II at ∼1525 cm–1 after hydrogen is substituted by deuterium; (b) curve-fitted Amide I of dehydrated egg case and (c) egg case in D2O, confirming the presence of β-sheets along with high α-helical content (>50%). Figure S6: Relative amounts of (a) hydrophobic and (b) charged amino acid residues at various heptad positions in the predicted coiled-coil domains of Bc-CPs and other known coil–coiled proteins in the CC+ database. Figure S7: Transmission electron micrographs of purified Bc-CPs. This material is available free of charge via the Internet at http://pubs.acs.org.

    Accession Codes

    The sequence data of Bc-CP 1a, Bc-CP 1b, Bc-CP 2, and Bc-CP 3 have been deposited in the NCBI database with the accession numbers GU205809, GU205810, GU205811, and GU205812, respectively.

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