Self-cyclisation as a general and efficient platform for peptide and protein macrocyclisation
Macrocyclisation of proteins and peptides results in a remarkable increase in structural stability, making cyclic peptides and proteins of great interest in drug discovery—either directly as drug leads or as in the case of cyclised nanodiscs (cNDs), as tools for studies of trans-membrane receptors a...
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Published in | Communications chemistry Vol. 6; no. 1; p. 48 |
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Main Authors | , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
London
Nature Publishing Group UK
04.03.2023
Nature Publishing Group Nature Portfolio |
Subjects | |
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Abstract | Macrocyclisation of proteins and peptides results in a remarkable increase in structural stability, making cyclic peptides and proteins of great interest in drug discovery—either directly as drug leads or as in the case of cyclised nanodiscs (cNDs), as tools for studies of trans-membrane receptors and membrane-active peptides. Various biological methods have been developed that are capable of yielding head-to-tail macrocyclised products. Recent advances in enzyme-catalysed macrocyclisation include discovery of new enzymes or design of new engineered enzymes. Here, we describe the engineering of a self-cyclising “
autocyclase
” protein, capable of performing a controllable unimolecular reaction for generation of cyclic biomolecules in high yield. We characterise the self-cyclisation reaction mechanism, and demonstrate how the unimolecular reaction path provides alternative avenues for addressing existing challenges in enzymatic cyclisation. We use the method to produce several notable cyclic peptides and proteins, demonstrating how autocyclases offer a simple, alternative way to access a vast diversity of macrocyclic biomolecules.
Head-to-tail macrocyclization of proteins and peptides can increase their structural stability, however, potential polymerization can lead to reduced yields. Here, the authors report the engineering of self-cyclizing ‘autocyclase’ proteins to generate macrocyclic peptides and proteins with favorable reaction kinetics for suppressing polymerization. |
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AbstractList | Head-to-tail macrocyclization of proteins and peptides can increase their structural stability, however, potential polymerization can lead to reduced yields. Here, the authors report the engineering of self-cyclizing ‘autocyclase’ proteins to generate macrocyclic peptides and proteins with favorable reaction kinetics for suppressing polymerization. Macrocyclisation of proteins and peptides results in a remarkable increase in structural stability, making cyclic peptides and proteins of great interest in drug discovery—either directly as drug leads or as in the case of cyclised nanodiscs (cNDs), as tools for studies of trans-membrane receptors and membrane-active peptides. Various biological methods have been developed that are capable of yielding head-to-tail macrocyclised products. Recent advances in enzyme-catalysed macrocyclisation include discovery of new enzymes or design of new engineered enzymes. Here, we describe the engineering of a self-cyclising “ autocyclase ” protein, capable of performing a controllable unimolecular reaction for generation of cyclic biomolecules in high yield. We characterise the self-cyclisation reaction mechanism, and demonstrate how the unimolecular reaction path provides alternative avenues for addressing existing challenges in enzymatic cyclisation. We use the method to produce several notable cyclic peptides and proteins, demonstrating how autocyclases offer a simple, alternative way to access a vast diversity of macrocyclic biomolecules. Macrocyclisation of proteins and peptides results in a remarkable increase in structural stability, making cyclic peptides and proteins of great interest in drug discovery—either directly as drug leads or as in the case of cyclised nanodiscs (cNDs), as tools for studies of trans-membrane receptors and membrane-active peptides. Various biological methods have been developed that are capable of yielding head-to-tail macrocyclised products. Recent advances in enzyme-catalysed macrocyclisation include discovery of new enzymes or design of new engineered enzymes. Here, we describe the engineering of a self-cyclising “ autocyclase ” protein, capable of performing a controllable unimolecular reaction for generation of cyclic biomolecules in high yield. We characterise the self-cyclisation reaction mechanism, and demonstrate how the unimolecular reaction path provides alternative avenues for addressing existing challenges in enzymatic cyclisation. We use the method to produce several notable cyclic peptides and proteins, demonstrating how autocyclases offer a simple, alternative way to access a vast diversity of macrocyclic biomolecules. Head-to-tail macrocyclization of proteins and peptides can increase their structural stability, however, potential polymerization can lead to reduced yields. Here, the authors report the engineering of self-cyclizing ‘autocyclase’ proteins to generate macrocyclic peptides and proteins with favorable reaction kinetics for suppressing polymerization. Macrocyclisation of proteins and peptides results in a remarkable increase in structural stability, making cyclic peptides and proteins of great interest in drug discovery-either directly as drug leads or as in the case of cyclised nanodiscs (cNDs), as tools for studies of trans-membrane receptors and membrane-active peptides. Various biological methods have been developed that are capable of yielding head-to-tail macrocyclised products. Recent advances in enzyme-catalysed macrocyclisation include discovery of new enzymes or design of new engineered enzymes. Here, we describe the engineering of a self-cyclising "autocyclase" protein, capable of performing a controllable unimolecular reaction for generation of cyclic biomolecules in high yield. We characterise the self-cyclisation reaction mechanism, and demonstrate how the unimolecular reaction path provides alternative avenues for addressing existing challenges in enzymatic cyclisation. We use the method to produce several notable cyclic peptides and proteins, demonstrating how autocyclases offer a simple, alternative way to access a vast diversity of macrocyclic biomolecules. Macrocyclisation of proteins and peptides results in a remarkable increase in structural stability, making cyclic peptides and proteins of great interest in drug discovery—either directly as drug leads or as in the case of cyclised nanodiscs (cNDs), as tools for studies of trans-membrane receptors and membrane-active peptides. Various biological methods have been developed that are capable of yielding head-to-tail macrocyclised products. Recent advances in enzyme-catalysed macrocyclisation include discovery of new enzymes or design of new engineered enzymes. Here, we describe the engineering of a self-cyclising “autocyclase” protein, capable of performing a controllable unimolecular reaction for generation of cyclic biomolecules in high yield. We characterise the self-cyclisation reaction mechanism, and demonstrate how the unimolecular reaction path provides alternative avenues for addressing existing challenges in enzymatic cyclisation. We use the method to produce several notable cyclic peptides and proteins, demonstrating how autocyclases offer a simple, alternative way to access a vast diversity of macrocyclic biomolecules.Head-to-tail macrocyclization of proteins and peptides can increase their structural stability, however, potential polymerization can lead to reduced yields. Here, the authors report the engineering of self-cyclizing ‘autocyclase’ proteins to generate macrocyclic peptides and proteins with favorable reaction kinetics for suppressing polymerization. |
ArticleNumber | 48 |
Author | Zhu, Yifei Crawford, Theo Chin, Yanni K.-Y. Zhang, Alan H. Stroet, Martin Thurecht, Kristofer J. Jia, Xinying Zhou, Zihan Hamilton, Brett R. Mobli, Mehdi Fletcher, Nicholas L. |
Author_xml | – sequence: 1 givenname: Xinying orcidid: 0000-0003-0133-8321 surname: Jia fullname: Jia, Xinying email: jiaxinying@gmail.com organization: Centre for Advanced Imaging, Australian Institute for Bioengineering & Nanotechnology, The University of Queensland – sequence: 2 givenname: Yanni K.-Y. surname: Chin fullname: Chin, Yanni K.-Y. organization: Centre for Advanced Imaging, Australian Institute for Bioengineering & Nanotechnology, The University of Queensland – sequence: 3 givenname: Alan H. surname: Zhang fullname: Zhang, Alan H. organization: Centre for Advanced Imaging, Australian Institute for Bioengineering & Nanotechnology, The University of Queensland – sequence: 4 givenname: Theo orcidid: 0000-0002-1101-5705 surname: Crawford fullname: Crawford, Theo organization: Centre for Advanced Imaging, Australian Institute for Bioengineering & Nanotechnology, The University of Queensland – sequence: 5 givenname: Yifei surname: Zhu fullname: Zhu, Yifei organization: Centre for Advanced Imaging, Australian Institute for Bioengineering & Nanotechnology, The University of Queensland – sequence: 6 givenname: Nicholas L. orcidid: 0000-0002-2993-833X surname: Fletcher fullname: Fletcher, Nicholas L. organization: Centre for Advanced Imaging, Australian Institute for Bioengineering & Nanotechnology, The University of Queensland – sequence: 7 givenname: Zihan surname: Zhou fullname: Zhou, Zihan organization: School of Chemistry and Molecular Biosciences, The University of Queensland – sequence: 8 givenname: Brett R. surname: Hamilton fullname: Hamilton, Brett R. organization: Centre for Advanced Imaging, Australian Institute for Bioengineering & Nanotechnology, The University of Queensland, Centre for Microscopy and Microanalysis, The University of Queensland – sequence: 9 givenname: Martin orcidid: 0000-0002-9570-2376 surname: Stroet fullname: Stroet, Martin organization: School of Chemistry and Molecular Biosciences, The University of Queensland – sequence: 10 givenname: Kristofer J. surname: Thurecht fullname: Thurecht, Kristofer J. organization: Centre for Advanced Imaging, Australian Institute for Bioengineering & Nanotechnology, The University of Queensland – sequence: 11 givenname: Mehdi orcidid: 0000-0003-2420-4262 surname: Mobli fullname: Mobli, Mehdi email: m.mobli@uq.edu.au organization: Centre for Advanced Imaging, Australian Institute for Bioengineering & Nanotechnology, The University of Queensland |
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Snippet | Macrocyclisation of proteins and peptides results in a remarkable increase in structural stability, making cyclic peptides and proteins of great interest in... Head-to-tail macrocyclization of proteins and peptides can increase their structural stability, however, potential polymerization can lead to reduced yields.... |
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SubjectTerms | 631/45/607/1166 631/45/611 631/92/607/1166 631/92/611 82/16 82/29 82/58 82/6 82/80 82/83 Biomolecules Chemistry Chemistry and Materials Science Chemistry/Food Science Controllability Enzymes Membranes Peptides Polymerization Proteins Reaction kinetics Reaction mechanisms Structural stability |
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Title | Self-cyclisation as a general and efficient platform for peptide and protein macrocyclisation |
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