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Simultaneous Control of Composition and Register of an AAB-Type Collagen Heterotrimer

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Department of Chemistry, Rice University, 6100 Main Street, Houston, Texas 77005, United States
Cite this: Biomacromolecules 2013, 14, 1, 179–185
Publication Date (Web):December 4, 2012
https://doi.org/10.1021/bm3015818
Copyright © 2012 American Chemical Society

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    Abstract

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    Control over composition and register of the peptide chains in AAB-type collagen mimetic heterotrimers is critical in developing systems that show fidelity to native collagen. However, their design is challenging due to the eight competing states possible for a mixture of nonidentical peptides A and B. Interpeptide salt-bridges have been used previously as keystone interactions to bias the population of competing states to favor a target heterotrimer. The designed heterotrimers were electroneutral and relied on pairing of acidic and basic residues but could not differentiate between all of the competing states and reported systems populated either multiple heterotrimer compositions or registers. Here our design methodology includes both positive and negative elements. First, an excess of acidic or basic residues, which always remain unpaired, introduces a negative design component to destabilize the competing triple helical compositions and registers. Second, charge pairs introduce a positive design component and stabilize the target assembly. These antagonistic factors are optimized in the target heterotrimer that forms the maximum number of charge pairs and minimizes unpaired charged residues. Additionally, we find that not just the number of paired and unpaired residues are important, but also the type. By a systematic study of different types of charge pairs and unpaired residues, we are able to populate a single composition-single register AAB heterotrimer. The insights gained here may be useful in designing composition and register specific heterotrimeric ligands with domains that recognize collagen-binding proteins.

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    HPLC chromatograms, ESI-mass spectra, and additional CD and NMR experiments. This material is available free of charge via the Internet at http://pubs.acs.org.

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    This article is cited by 21 publications.

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    13. Shumin Qiang, Cheng Lu, Fei Xu. Disrupting Effects of Osteogenesis Imperfecta Mutations Could Be Predicted by Local Hydrogen Bonding Energy. Biomolecules 2022, 12 (8) , 1104. https://doi.org/10.3390/biom12081104
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    16. Eric A. Chen, Yu-Shan Lin. Using synthetic peptides and recombinant collagen to understand DDR–collagen interactions. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 2019, 1866 (11) , 118458. https://doi.org/10.1016/j.bbamcr.2019.03.005
    17. Martin Köhler, Adrien Marchand, Nina B. Hentzen, Jasmine Egli, Alina I. Begley, Helma Wennemers, Renato Zenobi. Temperature-controlled electrospray ionization mass spectrometry as a tool to study collagen homo- and heterotrimers. Chemical Science 2019, 10 (42) , 9829-9835. https://doi.org/10.1039/C9SC03248G
    18. Yimin Qiu, Erik Poppleton, Arya Mekkat, Hongtao Yu, Sourav Banerjee, Sandra E. Wiley, Jack E. Dixon, David L. Kaplan, Yu-Shan Lin, Barbara Brodsky. Enzymatic Phosphorylation of Ser in a Type I Collagen Peptide. Biophysical Journal 2018, 115 (12) , 2327-2335. https://doi.org/10.1016/j.bpj.2018.11.012
    19. Andrew S. DiChiara, Rasia C. Li, Patreece H. Suen, Azade S. Hosseini, Rebecca J. Taylor, Alexander F. Weickhardt, Diya Malhotra, Darrell R. McCaslin, Matthew D. Shoulders. A cysteine-based molecular code informs collagen C-propeptide assembly. Nature Communications 2018, 9 (1) https://doi.org/10.1038/s41467-018-06185-2
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    21. Abhishek A Jalan, Jeffrey D Hartgerink. Pairwise interactions in collagen and the design of heterotrimeric helices. Current Opinion in Chemical Biology 2013, 17 (6) , 960-967. https://doi.org/10.1016/j.cbpa.2013.10.019

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