Structure, Biosynthesis, and Bioactivity of Photoditritide from Photorhabdus temperata Meg1

J Nat Prod. 2019 Dec 27;82(12):3499-3503. doi: 10.1021/acs.jnatprod.9b00932.

Lei Zhao ¹, Ryan Musumba Awori, Marcel Kaiser ², Jonathan Groß ³, Till Opatz ³, Helge B Bode

Affiliations

1 Institute of Botany, Jiangsu Province and Chinese Academy of Sciences , 210014 Nanjing , China.
2 Swiss Tropical and Public Health Institute , 4051 Basel , Switzerland.
3 Institute of Organic Chemistry , Johannes Gutenberg University Mainz , 55128 Mainz , Germany.

PMID: 31799840 DOI: 10.1021/acs.jnatprod.9b00932

Abstract

A new cyclic peptide photoditritide (1), containing two rare amino acid d-homoarginine residues, was isolated from Photorhabdus temperata Meg1 after the nonribosomal peptide synthetase encoding gene pdtS was activated via promoter exchange. The structure of 1 was elucidated by HR-MS and NMR experiments. The absolute configurations of Amino acids were determined according to the advanced Marfey's method after hydrolysis of 1. Bioactivity testing of 1 revealed potent antimicrobial activity against Micrococcus luteus with an MIC value of 3.0 μM and weak antiprotozoal activity against Trypanosoma brucei rhodesiense with an IC₅₀ value of 13 μM. Additionally, the biosynthetic pathway of 1 was also proposed.

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