Visible-light-mediated catalyst-free synthesis of unnatural α-amino acids and peptide macrocycles

Mengran Wang, Chao Wang, Yumei Huo, Xiaobo Dang, Hongxiang Xue, Liangyu Liu, Hongli Chai, Xiuling Xie, Zhixuan Li, Doudou Lu and Zhaoqing Xu ()
Additional contact information
Mengran Wang: Lanzhou University
Chao Wang: Lanzhou University
Yumei Huo: Lanzhou University
Xiaobo Dang: Lanzhou University
Hongxiang Xue: Lanzhou University
Liangyu Liu: Lanzhou University
Hongli Chai: Lanzhou University
Xiuling Xie: Lanzhou University
Zhixuan Li: Lanzhou University
Doudou Lu: Lanzhou University
Zhaoqing Xu: Lanzhou University

Nature Communications, 2021, vol. 12, issue 1, 1-9

Abstract: Abstract The visible light induced, photocatalysts or photoabsorbing EDA complexes mediated cleavage of pyridinium C-N bond were reported in the past years. Here, we report an ionic compound promote homolytic cleavage of pyridinium C-N bond by exploiting the photonic energy from visible light. This finding is successfully applied in deaminative hydroalkylation of a series of alkenes including naturally occurring dehydroalanine, which provides an efficient way to prepare β-alkyl substituted unnatural amino acids under mild and photocatalyst-free conditions. Importantly, by using this protocol, the deaminative cyclization of peptide backbone N-terminals is realized. Furthermore, the use of Et3N or PPh3 as reductants and H2O as hydrogen atom source is a practical advantage. We anticipate that our protocol will be useful in peptide synthesis and modern peptide drug discovery.

Date: 2021
References: View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-021-27086-x Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-27086-x

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-021-27086-x

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().