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Article: Total Synthesis of Malacidin A by β‐Hydroxyaspartic Acid Ligation‐Mediated Cyclization and Absolute Structure Establishment

TitleTotal Synthesis of Malacidin A by β‐Hydroxyaspartic Acid Ligation‐Mediated Cyclization and Absolute Structure Establishment
Authors
Issue Date2020
PublisherWiley - VCH Verlag GmbH & Co. KGaA. The Journal's web site is located at https://onlinelibrary.wiley.com/journal/15213773
Citation
Angewandte Chemie (International Edition), 2020, v. 59 n. 45, p. 19868-19872 How to Cite?
AbstractThe development of novel antibiotics is critical to combating the growing emergence of drug-resistant pathogens. Malacidin A is a new member of the calcium-dependent antibiotic (CDAs) family with activity against antibiotic-resistant pathogens. Its mode of action is distinct from classical CDAs. However, the absolute structure of malacidin A has not been established. Herein, the total syntheses of malacidin A and its analogues are reported by a combination of Fmoc-based solid-phase peptide synthesis (SPPS) and β-hydroxyaspartic acid ligation-mediated peptide cyclization. The total synthesis enabled us to establish the absolute configuration of malacidin A, which is in agreement with those for natural malacidin A confirmed by advanced Marfey's analysis in our study.
Persistent Identifierhttp://hdl.handle.net/10722/301377
ISSN
2023 Impact Factor: 16.1
2023 SCImago Journal Rankings: 5.300
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorSun, Z-
dc.contributor.authorShang, Z-
dc.contributor.authorForelli, N-
dc.contributor.authorPo, KHL-
dc.contributor.authorChen, S-
dc.contributor.authorBrady, SF-
dc.contributor.authorLi, X-
dc.date.accessioned2021-07-27T08:10:09Z-
dc.date.available2021-07-27T08:10:09Z-
dc.date.issued2020-
dc.identifier.citationAngewandte Chemie (International Edition), 2020, v. 59 n. 45, p. 19868-19872-
dc.identifier.issn1433-7851-
dc.identifier.urihttp://hdl.handle.net/10722/301377-
dc.description.abstractThe development of novel antibiotics is critical to combating the growing emergence of drug-resistant pathogens. Malacidin A is a new member of the calcium-dependent antibiotic (CDAs) family with activity against antibiotic-resistant pathogens. Its mode of action is distinct from classical CDAs. However, the absolute structure of malacidin A has not been established. Herein, the total syntheses of malacidin A and its analogues are reported by a combination of Fmoc-based solid-phase peptide synthesis (SPPS) and β-hydroxyaspartic acid ligation-mediated peptide cyclization. The total synthesis enabled us to establish the absolute configuration of malacidin A, which is in agreement with those for natural malacidin A confirmed by advanced Marfey's analysis in our study.-
dc.languageeng-
dc.publisherWiley - VCH Verlag GmbH & Co. KGaA. The Journal's web site is located at https://onlinelibrary.wiley.com/journal/15213773-
dc.relation.ispartofAngewandte Chemie (International Edition)-
dc.rightsSubmitted (preprint) Version This is the pre-peer reviewed version of the following article: [FULL CITE], which has been published in final form at [Link to final article using the DOI]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. Accepted (peer-reviewed) Version This is the peer reviewed version of the following article: [FULL CITE], which has been published in final form at [Link to final article using the DOI]. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions.-
dc.titleTotal Synthesis of Malacidin A by β‐Hydroxyaspartic Acid Ligation‐Mediated Cyclization and Absolute Structure Establishment-
dc.typeArticle-
dc.identifier.emailLi, X: xuechenl@hku.hk-
dc.identifier.authorityLi, X=rp00742-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1002/anie.202009092-
dc.identifier.pmid2725837-
dc.identifier.pmcidPMC8130013-
dc.identifier.scopuseid_2-s2.0-85089968853-
dc.identifier.hkuros323615-
dc.identifier.volume59-
dc.identifier.issue45-
dc.identifier.spage19868-
dc.identifier.epage19872-
dc.identifier.isiWOS:000564012500001-
dc.publisher.placeGermany-

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