Impact of oxetane incorporation on the structure and stability of alpha-helical peptides

Autor: Piotr Raubo, Jonathan D. Beadle, Rebecca Notman, Eleanor S. Jayawant, Ina Wilkening, Michael Shipman, Ann M. Dixon

Peptide-based drugs combine advantages of larger biological therapeutics with those of small molecule drugs, but they generally display poor permeability and metabolic stability. Recently, we introduced a new type of peptide bond isostere, in which t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::326bec79cda910845d6f2244132423fc
http://sro.sussex.ac.uk/id/eprint/108307/1/WRAP-macrocyclisation-small-peptides-enabled-oxetane-incorporation-Shipman-2018.pdf

Enzymatically-stable oxetane-based dipeptide hydrogels

Autor: Andrew G. Jamieson, Jonathan D. Beadle, Laura McDougall, Dave J. Adams, Emily R. Draper, Piotr Raubo, Michael Shipman

Publikováno v: Chemical Communications. 54:1793-1796

Low molecular weight gelators that are not easily degraded by enzymes have a range of potential applications. Here, we report new Fmoc-protected dipeptides in which the amide carbonyl group has been replaced by an oxetane ring. Remarkably one of thes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1529804255d4eef1486407a3886be9a
https://doi.org/10.1039/c7cc09701h

ChemInform Abstract: Synthesis of Oxetane- and Azetidine-Containing Spirocycles Related to the 2,5-Diketopiperazine Framework

Autor: Guy J. Clarkson, Michael Shipman, Piotr Raubo, Nicola H. Powell, Jonathan D. Beadle

Publikováno v: ChemInform. 47

A simple two-step sequence is used to efficiently make novel spirocyclic analogues of the diketopiperazine nucleus. Conjugate addition of chiral α-amino esters to nitroalkenes, generated from oxetan-3-one or N-Boc-azetidin-3-one, followed by nitro g

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1f7794ee9b68ddb03ad2bcbbdef1fbaf
https://doi.org/10.1002/chin.201623112

Engineering the structure of an N-terminal β-turn to maximize screw-sense preference in achiral helical peptide chains

Autor: Jonathan D. Beadle, Jordi Solà, Alejandro Castellanos, Thomas Boddaert, Robert A. Brown, Romina Wechsel, Jonathan Clayden, Liam Byrne, Matteo De Poli

Publikováno v: De Poli, M, Byrne, L, Brown, R A, Solà, J, Castellanos, A, Boddaert, T, Wechsel, R, Beadle, J D & Clayden, J 2014, ' Engineering the structure of an N-terminal β-turn to maximize screw-sense preference in achiral helical peptide chains ', Journal of Organic Chemistry, vol. 79, no. 10, pp. 4659-4675 . https://doi.org/10.1021/jo500714b

Oligomers of α-aminoisobutyric acid (Aib) are achiral peptides that typically adopt 310 helical conformations in which enantiomeric left- and right-handed conformers are, necessarily, equally populated. Incorporating a single protected chiral residu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00173acaec34d7ed0bc35793d73f8665
https://www.ccdc.cam.ac.uk/structures/search?id=doi:10.5517/cc11yx52&sid=DataCite