Evidence map›Paper›PMID 42435191›Full record

ArticleMolecular diversity2026

Discovery of potent biphenyl-macolacin derivatives through a lysine-T/CDHA iterative scanning (LTIS) strategy followed by chemical ligation-based modifications.

Xiaoshu Jing, Kaixuan Song, Biyao Liu, Kang Jin

Abstract read
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Article in Molecular diversity, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Xiaoshu Jing *Shandong Academy of Grape, Shandong Academy of Agricultural Sciences, Jinan, 250100, Shandong, China.
Kaixuan Song *Department of Medicinal Chemistry, State Key Laboratory of Discovery and Utilization of Functional Components in Traditional Chinese Medicine, School of Pharmaceutical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, 250012, Shandong, China.
Biyao LiuEngineering Research Center for Sugar and Sugar Complex, National-Local Joint Engineering Laboratory of Polysaccharide Drugs, Key Laboratory of Carbohydrate and Glycoconjugate Drugs, Shandong Academy of Pharmaceutical Science, Jinan, 250101, Shandong, China.
Kang JinDepartment of Medicinal Chemistry, State Key Laboratory of Discovery and Utilization of Functional Components in Traditional Chinese Medicine, School of Pharmaceutical Sciences, Cheeloo College of Medicine, Shandong University, Jinan, 250012, Shandong, China. jinkang@sdu.edu.cn.

Funding

Natural Science Foundation of Shandong Province ZR2025MS1237Shandong Provincial Key Research and Development Program (Major Technological Innovation Project) 2021CXGC010501the National Natural Science Foundation of China 22007059
6 · The paper itself

Abstract

The antibiotic biphenyl-macolacin (Bip-macolacin) is a promising drug candidate with good activity against Gram-negative bacteria including several colistin-resistant pathogens, providing a potential structural motif for developing novel antibiotics. Considering the importance of efficient and effective structural optimization in medicinal chemistry studies, we herein report a lysine-T/CDHA iterative scanning (LTIS) strategy to produce Bip-macolacin analogues and identify the modifiable sites, followed by structural derivatization through chemical ligation chemistry. Using this approach, four classes of Bip-macolacin derivatives were prepared conveniently, several of which exhibited antibacterial activities comparable or better than those of Bip-macolacin. The efficacy of representative analogues 5, 18, and 46 was also demonstrated by the resistance development evaluation and hemolysis assay. From this study, a systematic structure-activity relationship of Bip-macolacin was established as a reference for further development of Bip-macolacin-based antibiotics. This novel and powerful strategy also provides more opportunities and valuable options for the structural optimization in future research on peptide therapeutics.

Indexed as

Anti-Bacterial AgentsBiphenyl CompoundsDrug DiscoveryLysinePeptides, CyclicHemolysisMicrobial Sensitivity TestsStructure-Activity RelationshipAnti-Bacterial AgentsbiphenylBiphenyl CompoundsLysinePeptides, CyclicBiphenyl-macolacinChemical ligationCyclopeptide antibioticsNatural product synthesisStructural optimizationStructure-activity relationship

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.