Abstract：
:Peptaibols are linear non ribosomal peptides which have been the object of intense research efforts regarding their synthesis and the elucidation of the mechanism allowing their insertion in biological membranes. Forty years after their discovery they are still considered as model compounds and suitable probes for the investigation of new approaches aiming to test the efficacy of new coupling reagents, to physically and spectroscopically investigate the way by which they interact with the lipid bilayer and to develop artificial membrane pores. The stable helical secondary structure adopted by the peptaibols turn to be an adequate platform for gaining insight on the structural modifications induced by the substitution of the amide bond by 1,2,3-triazoles, but also for monitoring the impact of newly designed α,α-dialkyl glycine with fluorinated and silylated side chains as 2-aminoisobutyric acid mimic. Peptaibols secondary structure dictated by Aib high content has inspired the development of foldamers. Challenges and investigations on the above mentioned topics are discussed in this brief review.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Das S,Ben Haj Salah K,Djibo M,Inguimbert Ndoi
10.1016/j.abb.2018.09.016subject
Has Abstractpub_date
2018-11-15 00:00:00pages
16-30eissn
0003-9861issn
1096-0384pii
S0003-9861(18)30500-9journal_volume
658pub_type
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