{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,20]],"date-time":"2026-04-20T21:52:54Z","timestamp":1776721974560,"version":"3.51.2"},"reference-count":38,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2021,1,22]],"date-time":"2021-01-22T00:00:00Z","timestamp":1611273600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Research and Development and Innovation Office of Hungary","award":["K119509"],"award-info":[{"award-number":["K119509"]}]},{"DOI":"10.13039\/501100008530","name":"European Regional Development Fund","doi-asserted-by":"publisher","award":["GINOP-2.3.3-15-2016-00004"],"award-info":[{"award-number":["GINOP-2.3.3-15-2016-00004"]}],"id":[{"id":"10.13039\/501100008530","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100008530","name":"European Regional Development Fund","doi-asserted-by":"publisher","award":["GINOP-2.3.2-15-2016-00008"],"award-info":[{"award-number":["GINOP-2.3.2-15-2016-00008"]}],"id":[{"id":"10.13039\/501100008530","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pharmaceuticals"],"abstract":"<jats:p>For some time, glycopeptide antibiotics have been considered the last line of defense against Methicillin-resistant Staphylococcus aureus (MRSA). However, vancomycin resistance of Gram-positive bacteria is an increasingly emerging worldwide health problem. The mode of action of glycopeptide antibiotics is essentially the binding of peptidoglycan cell-wall fragments terminating in the d-Ala-d-Ala sequence to the carboxylate anion binding pocket of the antibiotic. Dimerization of these antibiotics in aqueous solution was shown to persist and even to enhance the antibacterial effect in a co-operative manner. Some works based on solid state (ss) Nuclear Magnetic Resonance (NMR) studies questioned the presence of dimers under the conditions of ssNMR while in a few cases, higher-order oligomers associated with contiguous back-to-back and face-to-face dimers were observed in the crystal phase. However, it is not proved if such oligomers persist in aqueous solutions. With the aid of 15N-labelled eremomycin using 15N relaxation and diffusion NMR methods, we observed tetramers and octamers when the N-Ac-d-Ala-d-Ala dipeptide was added. To the contrary, the N-Ac-d-Ala or (N-Ac)2-l-Lys-d-Ala-d-Ala tripeptide did not induce higher-order oligomers. These observations are interesting examples of tailored supramolecular self-organization. New antimicrobial tests have also been carried out with these self-assemblies against MRSA and VRE (resistant) strains.<\/jats:p>","DOI":"10.3390\/ph14020083","type":"journal-article","created":{"date-parts":[[2021,1,22]],"date-time":"2021-01-22T11:13:53Z","timestamp":1611314033000},"page":"83","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["Bacterial Cell Wall Analogue Peptides Control the Oligomeric States and Activity of the Glycopeptide Antibiotic Eremomycin: Solution NMR and Antimicrobial Studies"],"prefix":"10.3390","volume":"14","author":[{"given":"L\u00e1szl\u00f3","family":"Izs\u00e9pi","sequence":"first","affiliation":[{"name":"Doctoral School of Chemistry, University of Debrecen, H-4032 Debrecen, Egyetem t\u00e9r 1., Hungary"},{"name":"Department of Organic Chemistry, University of Debrecen, H-4032 Debrecen, Egyetem t\u00e9r 1., Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"R\u00e9ka","family":"Erdei","sequence":"additional","affiliation":[{"name":"Department of Organic Chemistry, University of Debrecen, H-4032 Debrecen, Egyetem t\u00e9r 1., Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1091-1011","authenticated-orcid":false,"given":"Anna N.","family":"Tevyashova","sequence":"additional","affiliation":[{"name":"Gause Institute of New Antibiotics, 11 B. Pirogovskaya, 119021 Moscow, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Natalia E.","family":"Grammatikova","sequence":"additional","affiliation":[{"name":"Gause Institute of New Antibiotics, 11 B. Pirogovskaya, 119021 Moscow, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6595-0811","authenticated-orcid":false,"given":"Andrey E.","family":"Shchekotikhin","sequence":"additional","affiliation":[{"name":"Gause Institute of New Antibiotics, 11 B. Pirogovskaya, 119021 Moscow, Russia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"P\u00e1l","family":"Herczegh","sequence":"additional","affiliation":[{"name":"Department of Pharmaceutical Chemistry, University of Debrecen, H-4032 Debrecen, Egyetem t\u00e9r 1., Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0442-1828","authenticated-orcid":false,"given":"Gyula","family":"Batta","sequence":"additional","affiliation":[{"name":"Department of Organic Chemistry, University of Debrecen, H-4032 Debrecen, Egyetem t\u00e9r 1., Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2021,1,22]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"R109","DOI":"10.1016\/S1074-5521(00)00116-2","article-title":"Vancomycin resistance in enterococci: Reprogramming of the D-Ala-D-Ala ligases in bacterial peptidoglycan biosynthesis","volume":"7","author":"Healy","year":"2000","journal-title":"Chem. 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