{"entity": "researcher", "timestamp": "2026-08-13T18:13:47.466Z", "family": "Wieske", "given": "Lianne H E", "initials": "LHE", "orcid": "0000-0003-4617-7605", "affiliations": ["Department of Chemistry-BMC, Uppsala University, 75123, Uppsala, Sweden."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/9ee9a8547a194235a4d32170996b53e9.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/9ee9a8547a194235a4d32170996b53e9"}}, "publications": [{"entity": "publication", "iuid": "d88276ac569d4cd0bd561502c908ae43", "links": {"self": {"href": "https://publications.scilifelab.se/publication/d88276ac569d4cd0bd561502c908ae43.json"}, "display": {"href": "https://publications.scilifelab.se/publication/d88276ac569d4cd0bd561502c908ae43"}}, "title": "Impact of Linker Composition on VHL PROTAC Cell Permeability.", "authors": [{"family": "Abeje", "given": "Yordanos Esubalew", "initials": "YE"}, {"family": "Wieske", "given": "Lianne H E", "initials": "LHE", "orcid": "0000-0003-4617-7605", "researcher": {"href": "https://publications.scilifelab.se/researcher/9ee9a8547a194235a4d32170996b53e9.json"}}, {"family": "Poongavanam", "given": "Vasanthanathan", "initials": "V", "orcid": "0000-0002-8880-9247", "researcher": {"href": "https://publications.scilifelab.se/researcher/d037f230665c490dada0a50ecc8c106f.json"}}, {"family": "Maassen", "given": "Stefanie", "initials": "S"}, {"family": "Atilaw", "given": "Yoseph", "initials": "Y"}, {"family": "Cromm", "given": "Philipp", "initials": "P"}, {"family": "Lehmann", "given": "Lutz", "initials": "L"}, {"family": "Erdelyi", "given": "Mate", "initials": "M", "orcid": "0000-0003-0359-5970", "researcher": {"href": "https://publications.scilifelab.se/researcher/f772b571449e417ca6fda2eee361a0c3.json"}}, {"family": "Meibom", "given": "Daniel", "initials": "D", "orcid": "0000-0003-4978-9842", "researcher": {"href": "https://publications.scilifelab.se/researcher/3034131b5fc94a24b8ab1a350205d960.json"}}, {"family": "Kihlberg", "given": "Jan", "initials": "J", "orcid": "0000-0002-4205-6040", "researcher": {"href": "https://publications.scilifelab.se/researcher/f9805d4f39cc48f79a6e6ba076917021.json"}}], "type": "journal article", "published": "2025-01-09", "journal": {"title": "J. Med. Chem.", "issn": "1520-4804", "volume": "68", "issue": "1", "pages": "638-657", "issn-l": "0022-2623"}, "abstract": "The discovery of cell permeable and orally bioavailable von Hippel-Lindau (VHL) proteolysis targeting chimeras (PROTACs) is challenging as their structures locates them at, or beyond, the outer limits of oral druggable space. We have designed a set of nine VHL PROTACs and found that the linker had a profound impact on passive cell permeability. Determination of the solution ensembles in a nonpolar solvent revealed that high permeability was correlated to the ability of the PROTACs to adopt folded conformations that have a low solvent accessible 3D polar surface area. Our results suggest that the design of cell permeable VHL PROTACs could focus on linkers that facilitate shielding of polar surface area in the VHL ligand in a nonpolar but not in a polar environment. In addition, we found that not only intramolecular hydrogen bonds, but also NH-\u03c0 and \u03c0-\u03c0 interactions contribute to the stabilization of low-polarity conformations, and thereby to high cell permeability.", "doi": "10.1021/acs.jmedchem.4c02492", "pmid": "39693386", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [{"db": "pmc", "key": "PMC11726670"}], "notes": [], "created": "2025-11-27T08:14:24.112Z", "modified": "2025-11-27T08:14:24.481Z"}, {"entity": "publication", "iuid": "f890cbfcb3e2469598263044fb5b9b8f", "links": {"self": {"href": "https://publications.scilifelab.se/publication/f890cbfcb3e2469598263044fb5b9b8f.json"}, "display": {"href": "https://publications.scilifelab.se/publication/f890cbfcb3e2469598263044fb5b9b8f"}}, "title": "The Influence of Disulfide, Thioacetal and Lanthionine-Bridges on the Conformation of a Macrocyclic Peptide.", "authors": [{"family": "Darling", "given": "William T P", "initials": "WTP", "orcid": "0009-0009-3161-8210", "researcher": {"href": "https://publications.scilifelab.se/researcher/c31a37663ab34a4a902fe0f406c0e761.json"}}, {"family": "Wieske", "given": "Lianne H E", "initials": "LHE", "orcid": "0000-0003-4617-7605", "researcher": {"href": "https://publications.scilifelab.se/researcher/9ee9a8547a194235a4d32170996b53e9.json"}}, {"family": "Cook", "given": "Declan T", "initials": "DT", "orcid": "0009-0006-4015-2545", "researcher": {"href": "https://publications.scilifelab.se/researcher/5c079317b3ab4e40b5514340f171b7b0.json"}}, {"family": "Aliev", "given": "Abil E", "initials": "AE", "orcid": "0000-0001-8725-3550", "researcher": {"href": "https://publications.scilifelab.se/researcher/a0b7706647034f83a000bee60f87e6f9.json"}}, {"family": "Caron", "given": "Laurent", "initials": "L"}, {"family": "Humphrys", "given": "Emily J", "initials": "EJ"}, {"family": "Figueiredo", "given": "Angelo Miguel", "initials": "AM", "orcid": "0000-0001-7039-5341", "researcher": {"href": "https://publications.scilifelab.se/researcher/e6442b5d89864dd4a1dfe6c1701529db.json"}}, {"family": "Hansen", "given": "D Flemming", "initials": "DF", "orcid": "0000-0003-0891-220X", "researcher": {"href": "https://publications.scilifelab.se/researcher/c46b312239f344e1bae145aa591151f3.json"}}, {"family": "Erd\u00e9lyi", "given": "M\u00e1t\u00e9", "initials": "M", "orcid": "0000-0003-0359-5970", "researcher": {"href": "https://publications.scilifelab.se/researcher/f772b571449e417ca6fda2eee361a0c3.json"}}, {"family": "Tabor", "given": "Alethea B", "initials": "AB", "orcid": "0000-0001-8216-0347", "researcher": {"href": "https://publications.scilifelab.se/researcher/7fd64bbc245c4effa4ae70b49cfec7ec.json"}}], "type": "journal article", "published": "2024-09-05", "journal": {"title": "Chemistry", "issn": "1521-3765", "volume": "30", "issue": "50", "pages": "e202401654", "issn-l": "0947-6539"}, "abstract": "Cyclisation of peptides by forming thioether (lanthionine), disulfide (cystine) or methylene thioacetal bridges between side chains is established as an important tool to stabilise a given structure, enhance metabolic stability and optimise both potency and selectivity. However, a systematic comparative study of the effects of differing bridging modalities on peptide conformation has not previously been carried out. In this paper, we have used the NMR deconvolution algorithm, NAMFIS, to determine the conformational ensembles, in aqueous solution, of three cyclic analogues of angiotensin(1-7), incorporating either disulfide, or non-reducible thioether or methylene thioacetal bridges. We demonstrate that the major solution conformations are conserved between the different bridged peptides, but the distribution of conformations differs appreciably. This suggests that subtle differences in ring size and bridging structure can be exploited to fine-tune the conformational properties of cyclic peptides, which may modulate their bioactivities.", "doi": "10.1002/chem.202401654", "pmid": "38953277", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [], "notes": [], "created": "2024-11-28T14:38:06.602Z", "modified": "2025-10-17T13:03:52.776Z"}, {"entity": "publication", "iuid": "7b80799f2d09404081e5bb56c978770b", "links": {"self": {"href": "https://publications.scilifelab.se/publication/7b80799f2d09404081e5bb56c978770b.json"}, "display": {"href": "https://publications.scilifelab.se/publication/7b80799f2d09404081e5bb56c978770b"}}, "title": "Taming Molecular Folding: Anion-Templated Foldamers with Tunable Quaternary Structures.", "authors": [{"family": "John", "given": "Eric A", "initials": "EA"}, {"family": "Riel", "given": "Asia Marie S", "initials": "AMS"}, {"family": "Wieske", "given": "Lianne H E", "initials": "LHE", "orcid": "0000-0003-4617-7605", "researcher": {"href": "https://publications.scilifelab.se/researcher/9ee9a8547a194235a4d32170996b53e9.json"}}, {"family": "Ray", "given": "Debmalya", "initials": "D"}, {"family": "Decato", "given": "Daniel A", "initials": "DA"}, {"family": "Boller", "given": "Madeleine", "initials": "M"}, {"family": "Takacs", "given": "Zoltan", "initials": "Z"}, {"family": "Erd\u00e9lyi", "given": "M\u00e1t\u00e9", "initials": "M", "orcid": "0000-0003-0359-5970", "researcher": {"href": "https://publications.scilifelab.se/researcher/f772b571449e417ca6fda2eee361a0c3.json"}}, {"family": "Bryantsev", "given": "Vyacheslav S", "initials": "VS", "orcid": "0000-0002-6501-6594", "researcher": {"href": "https://publications.scilifelab.se/researcher/0bbc97e2dbae4ba09b82c1047846d4ee.json"}}, {"family": "Berryman", "given": "Orion B", "initials": "OB", "orcid": "0000-0002-0324-484X", "researcher": {"href": "https://publications.scilifelab.se/researcher/061741875e4b4e818a8298896f0de328.json"}}], "type": "journal article", "published": "2024-06-06", "journal": {"title": "J. Am. Chem. Soc.", "issn": "1520-5126", "issn-l": "0002-7863"}, "abstract": "Higher-order foldamers represent a unique class of supramolecules at the forefront of molecular design. Herein we control quaternary folding using a novel approach that combines halogen bonding (XBing) and hydrogen bonding (HBing). We present the first anion-templated double helices induced by halogen bonds (XBs) and stabilized by \"hydrogen bond enhanced halogen bonds\" (HBeXBs). Our findings demonstrate that the number and orientation of hydrogen bond (HB) and XB donors significantly affect the quaternary structure and guest selectivity of two similar oligomers. This research offers new design elements to engineer foldamers and tailor their quaternary structure for specific guest binding.", "doi": "10.1021/jacs.3c14820", "pmid": "38842125", "labels": {"Swedish NMR Centre": "Collaborative"}, "xrefs": [], "notes": [], "created": "2024-11-28T14:36:34.288Z", "modified": "2025-10-17T13:03:52.929Z"}, {"entity": "publication", "iuid": "3355c650475e4ce5881d5835cff6729e", "links": {"self": {"href": "https://publications.scilifelab.se/publication/3355c650475e4ce5881d5835cff6729e.json"}, "display": {"href": "https://publications.scilifelab.se/publication/3355c650475e4ce5881d5835cff6729e"}}, "title": "NMR Backbone Assignment of VIM-2 and Identification of the Active Enantiomer of a Potential Inhibitor", "authors": [{"family": "Wieske", "given": "Lianne H E", "initials": "LHE", "orcid": "0000-0003-4617-7605", "researcher": {"href": "https://publications.scilifelab.se/researcher/9ee9a8547a194235a4d32170996b53e9.json"}}, {"family": "Bogaerts", "given": "Jonathan", "initials": "J", "orcid": "0000-0001-8089-7759", "researcher": {"href": "https://publications.scilifelab.se/researcher/921da51be41e4b41b3b3499ae7cc61d6.json"}}, {"family": "Leding", "given": "Albin A M", "initials": "AAM", "orcid": "0000-0003-1071-6929", "researcher": {"href": "https://publications.scilifelab.se/researcher/6d765f3a2bcd4957ab279471c1dd4fa9.json"}}, {"family": "Wilcox", "given": "Scott", "initials": "S"}, {"family": "Andersson Rasmussen", "given": "Anna", "initials": "A"}, {"family": "Leszczak", "given": "Kinga", "initials": "K"}, {"family": "Turunen", "given": "Lotta", "initials": "L"}, {"family": "Herrebout", "given": "Wouter A", "initials": "WA", "orcid": "0000-0002-3167-8944", "researcher": {"href": "https://publications.scilifelab.se/researcher/bba405b9bce14713a0635a6999f7666a.json"}}, {"family": "Hubert", "given": "Madlen", "initials": "M"}, {"family": "Bayer", "given": "Annette", "initials": "A", "orcid": "0000-0003-3481-200X", "researcher": {"href": "https://publications.scilifelab.se/researcher/e921a3a52ec047cdae2961e37a4aac46.json"}}, {"family": "Erd\u00e9lyi", "given": "M\u00e1t\u00e9", "initials": "M", "orcid": "0000-0003-0359-5970", "researcher": {"href": "https://publications.scilifelab.se/researcher/f772b571449e417ca6fda2eee361a0c3.json"}}], "type": "journal-article", "published": "2022-02-10", "journal": {"title": "ACS Med Chem Lett", "issn": "1948-5875", "volume": "13", "issue": "2", "pages": "257-261", "issn-l": "1948-5875"}, "abstract": null, "doi": "10.1021/acsmedchemlett.1c00635", "pmid": null, "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [], "notes": [], "created": "2022-04-25T12:00:22.113Z", "modified": "2025-10-17T13:03:55.008Z"}, {"entity": "publication", "iuid": "5d12d628f2724cf0ad933f301dbf3d4f", "links": {"self": {"href": "https://publications.scilifelab.se/publication/5d12d628f2724cf0ad933f301dbf3d4f.json"}, "display": {"href": "https://publications.scilifelab.se/publication/5d12d628f2724cf0ad933f301dbf3d4f"}}, "title": "Non-uniform sampling for NOESY? A case study on spiramycin.", "authors": [{"family": "Wieske", "given": "Lianne H E", "initials": "LHE", "orcid": "0000-0003-4617-7605", "researcher": {"href": "https://publications.scilifelab.se/researcher/9ee9a8547a194235a4d32170996b53e9.json"}}, {"family": "Erd\u00e9lyi", "given": "M\u00e1t\u00e9", "initials": "M", "orcid": "0000-0003-0359-5970", "researcher": {"href": "https://publications.scilifelab.se/researcher/f772b571449e417ca6fda2eee361a0c3.json"}}], "type": "journal article", "published": "2021-07-00", "journal": {"title": "Magn Reson Chem", "issn": "0749-1581", "volume": "59", "issue": "7", "pages": "723-737", "issn-l": null}, "abstract": "To date, most nuclear magnetic resonance (NMR)-based 3-D structure determinations of both small molecules and of biopolymers utilize the nuclear Overhauser effect (NOE) via NOESY spectra. The acquisition of high-quality NOESY spectra is a prerequisite for quantitative analysis providing accurate interatomic distances. As the acquisition of NOE build-ups is time-consuming, acceleration of the process by the use of non-uniform sampling (NUS) may seem beneficial; however, the quantitativity of NOESY spectra acquired with NUS has not yet been validated. Herein, NOESY spectra with various extents of NUS have been recorded, artificial NUS spectra with two different sampling schemes created, and by using two different NUS reconstruction algorithms the influence of NUS on the data quality was evaluated. Using statistical analyses, NUS is demonstrated to influence the accuracy of quantitative NOE experiments. The NOE-based distances show an increased error as the sampling density decreases. Weak NOE signals are affected more severely by NUS than more intense ones. The application of NUS with NOESY comes at two major costs: the interatomic distances are determined with lower accuracy and long-range correlations are lost.", "doi": "10.1002/mrc.5133", "pmid": "33469934", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [], "notes": [], "created": "2021-07-02T14:03:19.065Z", "modified": "2025-10-17T13:03:55.765Z"}, {"entity": "publication", "iuid": "183a39b655614a3faef837da3a14521b", "links": {"self": {"href": "https://publications.scilifelab.se/publication/183a39b655614a3faef837da3a14521b.json"}, "display": {"href": "https://publications.scilifelab.se/publication/183a39b655614a3faef837da3a14521b"}}, "title": "Solution Conformations Explain the Chameleonic Behaviour of Macrocyclic Drugs.", "authors": [{"family": "Danelius", "given": "Emma", "initials": "E", "orcid": "0000-0002-7322-9661", "researcher": {"href": "https://publications.scilifelab.se/researcher/738da5a280d04d3b9b1ced257b9ddb7f.json"}}, {"family": "Poongavanam", "given": "Vasanthanathan", "initials": "V", "orcid": "0000-0002-8880-9247", "researcher": {"href": "https://publications.scilifelab.se/researcher/d037f230665c490dada0a50ecc8c106f.json"}}, {"family": "Peintner", "given": "Stefan", "initials": "S", "orcid": "0000-0001-9882-2018", "researcher": {"href": "https://publications.scilifelab.se/researcher/0583434982c84bd69f313f713744f5ed.json"}}, {"family": "Wieske", "given": "Lianne H E", "initials": "LHE", "orcid": "0000-0003-4617-7605", "researcher": {"href": "https://publications.scilifelab.se/researcher/9ee9a8547a194235a4d32170996b53e9.json"}}, {"family": "Erd\u00e9lyi", "given": "M\u00e1t\u00e9", "initials": "M", "orcid": "0000-0003-0359-5970", "researcher": {"href": "https://publications.scilifelab.se/researcher/f772b571449e417ca6fda2eee361a0c3.json"}}, {"family": "Kihlberg", "given": "Jan", "initials": "J", "orcid": "0000-0002-4205-6040", "researcher": {"href": "https://publications.scilifelab.se/researcher/f9805d4f39cc48f79a6e6ba076917021.json"}}], "type": "journal article", "published": "2020-04-21", "journal": {"title": "Chemistry", "issn": "1521-3765", "volume": "26", "issue": "23", "pages": "5231-5244", "issn-l": "0947-6539"}, "abstract": "It has been hypothesised that drugs in the chemical space \"beyond the rule of 5\" (bRo5) must behave as molecular chameleons to combine otherwise conflicting properties, including aqueous solubility, cell permeability and target binding. Evidence for this has, however, been limited to the cyclic peptide cyclosporine A. Herein, we show that the non-peptidic and macrocyclic drugs roxithromycin, telithromycin and spiramycin behave as molecular chameleons, with rifampicin showing a less pronounced behaviour. In particular roxithromycin, telithromycin and spiramycin display a marked, yet limited flexibility and populate significantly less polar and more compact conformational ensembles in an apolar than in a polar environment. In addition to balancing of membrane permeability and aqueous solubility, this flexibility also allows binding to targets that vary in structure between species. The drugs' passive cell permeability correlates to their 3D polar surface area and corroborate two theoretical models for permeability, developed for cyclic peptides. We conclude that molecular chameleonicity should be incorporated in the design of orally administered drugs in the bRo5 space.", "doi": "10.1002/chem.201905599", "pmid": "32027758", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [], "notes": [], "created": "2020-12-11T09:13:45.140Z", "modified": "2025-10-17T13:03:56.989Z"}]}