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  1. Article ; Online: Late-Stage Functionalization of Living Organisms: Rethinking Selectivity in Biology.

    Giltrap, Andrew M / Yuan, Yizhi / Davis, Benjamin G

    Chemical reviews

    2024  Volume 124, Issue 3, Page(s) 889–928

    Abstract: With unlimited selectivity, full post-translational chemical control of biology would circumvent the dogma of genetic control. The resulting direct manipulation of organisms would enable atomic-level precision in "editing" of function. We argue that a ... ...

    Abstract With unlimited selectivity, full post-translational chemical control of biology would circumvent the dogma of genetic control. The resulting direct manipulation of organisms would enable atomic-level precision in "editing" of function. We argue that a key aspect that is still missing in our ability to do this (at least with a high degree of control) is the selectivity of a given chemical reaction in a living organism. In this Review, we systematize existing illustrative examples of chemical selectivity, as well as identify needed chemical selectivities set in a hierarchy of anatomical complexity: organismo- (selectivity for a given organism over another), tissuo- (selectivity for a given tissue type in a living organism), cellulo- (selectivity for a given cell type in an organism or tissue), and organelloselectivity (selectivity for a given organelle or discrete body within a cell). Finally, we analyze more traditional concepts such as regio-, chemo-, and stereoselective reactions where additionally appropriate. This survey of late-stage biomolecule methods emphasizes, where possible, functional consequences (
    MeSH term(s) Proteomics
    Language English
    Publishing date 2024-01-17
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 207949-5
    ISSN 1520-6890 ; 0009-2665
    ISSN (online) 1520-6890
    ISSN 0009-2665
    DOI 10.1021/acs.chemrev.3c00579
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  2. Article: Stereoretentive Post-Translational Protein Editing.

    Fu, Xia-Ping / Yuan, Yizhi / Jha, Ajay / Levin, Nikita / Giltrap, Andrew M / Ren, Jack / Mamalis, Dimitrios / Mohammed, Shabaz / Davis, Benjamin G

    ACS central science

    2023  Volume 9, Issue 3, Page(s) 405–416

    Abstract: Chemical post-translational methods allow convergent side-chain editing of proteins without needing to resort to genetic intervention. Current approaches that allow the creation of constitutionally native side chains via C-C bond formation, using off- ... ...

    Abstract Chemical post-translational methods allow convergent side-chain editing of proteins without needing to resort to genetic intervention. Current approaches that allow the creation of constitutionally native side chains via C-C bond formation, using off-protein carbon-centered C· radicals added to unnatural amino acid radical acceptor (SOMOphile, singly occupied molecular orbital (SOMO)) "tags" such as dehydroalanine, are benign and wide-ranging. However, they also typically create epimeric mixtures of d/l-residues. Here, we describe a light-mediated desulfurative method that, through the creation and reaction of stereoretained
    Language English
    Publishing date 2023-02-24
    Publishing country United States
    Document type Journal Article
    ISSN 2374-7943
    ISSN 2374-7943
    DOI 10.1021/acscentsci.2c00991
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  3. Article ; Online: Reductive site-selective atypical

    Mollner, Tim A / Giltrap, Andrew M / Zeng, Yibo / Demyanenko, Yana / Buchanan, Charles / Oehlrich, Daniel / Baldwin, Andrew J / Anthony, Daniel C / Mohammed, Shabaz / Davis, Benjamin G

    Science advances

    2022  Volume 8, Issue 14, Page(s) eabl8675

    Abstract: Biomolecule environments can enhance chemistries with the potential to mediate and modulate self-modification (e.g., self-cleavage). While these enhanced modes are found in certain biomolecules (e.g., RNA ribozymes), it is more rare in proteins. Targeted ...

    Abstract Biomolecule environments can enhance chemistries with the potential to mediate and modulate self-modification (e.g., self-cleavage). While these enhanced modes are found in certain biomolecules (e.g., RNA ribozymes), it is more rare in proteins. Targeted proteolytic cleavage is vital to physiology, biotechnology, and even emerging therapy. Yet, purely chemically induced methods for the site-selective cleavage of proteins remain scarce. Here, as a proof of principle, we designed and tested a system intended to combine protein-enhanced chemistry with tag modification to enable synthetic reductive protein chemistries promoted by diboron. This reductively driven, single-electron chemistry now enables an operationally simple, site-selective cleavage protocol for proteins directed to readily accessible dehydroalanine (Dha) residues as tags under aqueous conditions and in cell lysates. In this way, a mild, efficient, enzyme-free method now allows not only precise chemical proteolysis but also simultaneous use in the removal of affinity tags and/or protein-terminus editing to create altered N- and C-termini such as protein amidation (─CONH
    Language English
    Publishing date 2022-04-08
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.abl8675
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  4. Article ; Online: Total Synthesis and Antimycobacterial Activity of Ohmyungsamycin A, Deoxyecumicin, and Ecumicin.

    Hawkins, Paige M E / Tran, Wendy / Nagalingam, Gayathri / Cheung, Chen-Yi / Giltrap, Andrew M / Cook, Gregory M / Britton, Warwick J / Payne, Richard J

    Chemistry (Weinheim an der Bergstrasse, Germany)

    2020  Volume 26, Issue 66, Page(s) 15200–15205

    Abstract: The ohmyungsamycin and ecumicin natural product families are structurally related cyclic depsipeptides that display potent antimycobacterial activity. Herein the total syntheses of ohmyungsamycin A, deoxyecumicin, and ecumicin are reported, together with ...

    Abstract The ohmyungsamycin and ecumicin natural product families are structurally related cyclic depsipeptides that display potent antimycobacterial activity. Herein the total syntheses of ohmyungsamycin A, deoxyecumicin, and ecumicin are reported, together with the direct biological comparison of members of these natural product families against Mycobacterium tuberculosis (Mtb), the etiological agent of tuberculosis (TB). The synthesis of each of the natural products employed a solid-phase strategy to assemble the linear peptide precursor, involving a key on-resin esterification and an optional on-resin dimethylation step, before a final solution-phase macrolactamization between the non-proteinogenic N-methyl-4-methoxy-l-tryptophan amino acid and a bulky N-methyl-l-valine residue. The synthetic natural products possessed potent antimycobacterial activity against Mtb with MIC
    MeSH term(s) Antitubercular Agents/chemical synthesis ; Antitubercular Agents/chemistry ; Antitubercular Agents/pharmacology ; Humans ; Mycobacterium tuberculosis ; Peptides, Cyclic/chemical synthesis ; Peptides, Cyclic/chemistry ; Tuberculosis
    Chemical Substances Antitubercular Agents ; Peptides, Cyclic ; ecumicin ; ohmyungsamycin A
    Language English
    Publishing date 2020-10-22
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 1478547-X
    ISSN 1521-3765 ; 0947-6539
    ISSN (online) 1521-3765
    ISSN 0947-6539
    DOI 10.1002/chem.202002408
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  5. Article ; Online: Synthetic Studies Toward the Skyllamycins: Total Synthesis and Generation of Simplified Analogues.

    Giltrap, Andrew M / Haeckl, F P Jake / Kurita, Kenji L / Linington, Roger G / Payne, Richard J

    The Journal of organic chemistry

    2018  Volume 83, Issue 13, Page(s) 7250–7270

    Abstract: Herein, we report our synthetic studies toward the skyllamycins, a highly modified class of nonribosomal peptide natural products which contain a number of interesting structural features, including the extremely rare α-OH-glycine residue. Before ... ...

    Abstract Herein, we report our synthetic studies toward the skyllamycins, a highly modified class of nonribosomal peptide natural products which contain a number of interesting structural features, including the extremely rare α-OH-glycine residue. Before embarking on the synthesis of the natural products, we prepared four structurally simpler analogues. Access to both the analogues and the natural products first required the synthesis of a number of nonproteinogenic amino acids, including three β-OH amino acids that were accessed from the convenient chiral precursor Garner's aldehyde. Following the preparation of the suitably protected nonproteinogenic amino acids, the skyllamycin analogues were assembled using a solid-phase synthetic route followed by a final stage solution-phase cyclization reaction. To access the natural products (skyllamycins A-C) the synthetic route used for the analogues was modified. Specifically, linear peptide precursors containing a C-terminal amide were synthesized via solid-phase peptide synthesis. After cleavage from the resin the N-terminal serine residue was oxidatively cleaved to a glyoxyamide moiety. The target natural products, skyllamycins A-C, were successfully prepared via a final step cyclization with concomitant formation of the unusual α-OH-glycine residue. Purification and spectroscopic comparison to the authentic isolated material confirmed the identity of the synthetic natural products.
    Language English
    Publishing date 2018-06-11
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 123490-0
    ISSN 1520-6904 ; 0022-3263
    ISSN (online) 1520-6904
    ISSN 0022-3263
    DOI 10.1021/acs.joc.8b00898
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  6. Article ; Online: Total Synthesis of Ecumicin.

    Hawkins, Paige M E / Giltrap, Andrew M / Nagalingam, Gayathri / Britton, Warwick J / Payne, Richard J

    Organic letters

    2018  Volume 20, Issue 4, Page(s) 1019–1022

    Abstract: The first total synthesis of the potent anti-mycobacterial cyclic depsipeptide natural product ecumicin is described. Synthesis was achieved via a solid-phase strategy, incorporating the synthetic non-proteinogenic amino acids N-methyl-4-methoxy-l- ... ...

    Abstract The first total synthesis of the potent anti-mycobacterial cyclic depsipeptide natural product ecumicin is described. Synthesis was achieved via a solid-phase strategy, incorporating the synthetic non-proteinogenic amino acids N-methyl-4-methoxy-l-tryptophan and threo-β-hydroxy-l-phenylalanine into the growing linear peptide chain. The synthesis employed key on-resin esterification and dimethylation steps as well as a final macrolactamization between the unusual N-methyl-4-methoxy-l-tryptophan unit and a bulky N-methyl-l-valine residue. The synthetic natural product possessed potent antimycobacterial activity against the virulent H37Rv strain of Mycobacterium tuberculosis (MIC
    Language English
    Publishing date 2018--16
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1523-7052
    ISSN (online) 1523-7052
    DOI 10.1021/acs.orglett.7b03967
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  7. Article: Synthetic Studies Toward the Skyllamycins: Total Synthesis and Generation of Simplified Analogues

    Giltrap, Andrew M / F. P. Jake Haeckl / Kenji L. Kurita / Richard J. Payne / Roger G. Linington

    Journal of organic chemistry. 2018 May 25, v. 83, no. 13

    2018  

    Abstract: Herein, we report our synthetic studies toward the skyllamycins, a highly modified class of nonribosomal peptide natural products which contain a number of interesting structural features, including the extremely rare α-OH-glycine residue. Before ... ...

    Abstract Herein, we report our synthetic studies toward the skyllamycins, a highly modified class of nonribosomal peptide natural products which contain a number of interesting structural features, including the extremely rare α-OH-glycine residue. Before embarking on the synthesis of the natural products, we prepared four structurally simpler analogues. Access to both the analogues and the natural products first required the synthesis of a number of nonproteinogenic amino acids, including three β-OH amino acids that were accessed from the convenient chiral precursor Garner’s aldehyde. Following the preparation of the suitably protected nonproteinogenic amino acids, the skyllamycin analogues were assembled using a solid-phase synthetic route followed by a final stage solution-phase cyclization reaction. To access the natural products (skyllamycins A–C) the synthetic route used for the analogues was modified. Specifically, linear peptide precursors containing a C-terminal amide were synthesized via solid-phase peptide synthesis. After cleavage from the resin the N-terminal serine residue was oxidatively cleaved to a glyoxyamide moiety. The target natural products, skyllamycins A–C, were successfully prepared via a final step cyclization with concomitant formation of the unusual α-OH-glycine residue. Purification and spectroscopic comparison to the authentic isolated material confirmed the identity of the synthetic natural products.
    Keywords aldehydes ; cyclization reactions ; moieties ; organic chemistry ; serine ; spectroscopy
    Language English
    Dates of publication 2018-0525
    Size p. 7250-7270.
    Publishing place American Chemical Society
    Document type Article
    ZDB-ID 123490-0
    ISSN 1520-6904 ; 0022-3263
    ISSN (online) 1520-6904
    ISSN 0022-3263
    DOI 10.1021/acs.joc.8b00898
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  8. Article ; Online: Synthesis of β-Thiol Phenylalanine for Applications in One-Pot Ligation-Desulfurization Chemistry.

    Malins, Lara R / Giltrap, Andrew M / Dowman, Luke J / Payne, Richard J

    Organic letters

    2015  Volume 17, Issue 9, Page(s) 2070–2073

    Abstract: The efficient synthesis of a β-thiol phenylalanine derivative is described starting from Garner's aldehyde. The utility of this amino acid in peptide ligation-desulfurization chemistry is described, including the trifluoroethanethiol (TFET)-promoted one- ... ...

    Abstract The efficient synthesis of a β-thiol phenylalanine derivative is described starting from Garner's aldehyde. The utility of this amino acid in peptide ligation-desulfurization chemistry is described, including the trifluoroethanethiol (TFET)-promoted one-pot assembly of the 62 residue peptide hormone augurin.
    MeSH term(s) Aldehydes/chemistry ; Ligation ; Molecular Structure ; Neoplasm Proteins/chemistry ; Peptide Hormones/chemistry ; Peptides/chemistry ; Phenylalanine/analogs & derivatives ; Phenylalanine/chemical synthesis ; Phenylalanine/chemistry ; Sulfhydryl Compounds/chemical synthesis ; Sulfhydryl Compounds/chemistry ; Trifluoroethanol/analogs & derivatives ; Trifluoroethanol/chemistry
    Chemical Substances 2,2,2-trifluoroethanethiol ; Aldehydes ; ECRG4 protein, human ; Neoplasm Proteins ; Peptide Hormones ; Peptides ; Sulfhydryl Compounds ; Phenylalanine (47E5O17Y3R) ; Trifluoroethanol (75-89-8)
    Language English
    Publishing date 2015-04-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1523-7052
    ISSN (online) 1523-7052
    DOI 10.1021/acs.orglett.5b00597
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Total Synthesis of Skyllamycins A-C.

    Giltrap, Andrew M / Haeckl, F P Jake / Kurita, Kenji L / Linington, Roger G / Payne, Richard J

    Chemistry (Weinheim an der Bergstrasse, Germany)

    2017  Volume 23, Issue 60, Page(s) 15046–15049

    Abstract: The skyllamycins are a family of highly functionalized non-ribosomal cyclic depsipeptide natural products which contain the extremely rare α-OH-glycine functionality. Herein the first total synthesis of skyllamycins A-C is reported, together with the ... ...

    Abstract The skyllamycins are a family of highly functionalized non-ribosomal cyclic depsipeptide natural products which contain the extremely rare α-OH-glycine functionality. Herein the first total synthesis of skyllamycins A-C is reported, together with the biofilm inhibitory activity of the natural products. Linear peptide precursors for each natural product were prepared through an efficient solid-phase route incorporating a number of synthetic modified amino acids. A novel macrocyclization step between a C-terminal amide and an N-terminal glyoxylamide moiety served as a key transformation to install the unique α-OH-glycine unit and generate the natural products in the final step of the synthesis.
    Language English
    Publishing date 2017-10-26
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 1478547-x
    ISSN 1521-3765 ; 0947-6539
    ISSN (online) 1521-3765
    ISSN 0947-6539
    DOI 10.1002/chem.201704277
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  10. Article: Synthesis of β-Thiol Phenylalanine for Applications in One-Pot Ligation–Desulfurization Chemistry

    Malins, Lara R / Giltrap Andrew M / Dowman Luke J / Payne Richard J

    Organic letters. 2015 May 01, v. 17, no. 9

    2015  

    Abstract: The efficient synthesis of a β-thiol phenylalanine derivative is described starting from Garner’s aldehyde. The utility of this amino acid in peptide ligation–desulfurization chemistry is described, including the trifluoroethanethiol (TFET)-promoted ...

    Abstract The efficient synthesis of a β-thiol phenylalanine derivative is described starting from Garner’s aldehyde. The utility of this amino acid in peptide ligation–desulfurization chemistry is described, including the trifluoroethanethiol (TFET)-promoted one-pot assembly of the 62 residue peptide hormone augurin.
    Keywords aldehydes ; chemical reactions ; chemical structure ; phenylalanine
    Language English
    Dates of publication 2015-0501
    Size p. 2070-2073.
    Publishing place American Chemical Society
    Document type Article
    ISSN 1523-7052
    DOI 10.1021%2Facs.orglett.5b00597
    Database NAL-Catalogue (AGRICOLA)

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