Year: 2017
Type: article
Abstract: + 7 positions, respectively, were cyclised to introduce a diverse array of aryl and bi-aryl linkers. These two series of macrocyclic peptides displayed similar linker-dependent lipophilicity, phospholipid affinity, and unique volume of distributions. Additionally, one of the bioactive peptides showed target binding affinity that was predominantly affected by the length of the linker. Collectively, this divergent strategy allowed rapid and convenient access to various aryl linkers, enabling the systematic evaluation of the effect of appending unit on the medicinal properties of macrocyclic peptides.
Source: Chemical Science
DOI: 10.1039/c6sc05454d
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: diamond
Funders: National Science Foundation, Damon Runyon Cancer Research Foundation, Bristol-Myers Squibb, Sontag Foundation, Massachusetts Institute of Technology, National Institutes of Health, National Institute of General Medical Sciences, National Institute of Environmental Health Sciences, Division of Chemistry
Awards: G1355488677, G1766776992, MIT Center for Environmental Health Sciences, G5269294086, CATALYTIC METHODS FOR ORGANIC SYNTHESIS, Modernization of a 500 MHz NMR Instrument, Acquisition of Octet Biolayer Interferometry system for MIT biophysics facility, Cysteine Arylation, Catalytic Methods for Organic Synthesis, G9000204311, G9000236517, Metal-Catalyzed Methods for Organic Synthesis
OpenAlex ID: W2599690337