2015
DOI: 10.1021/acs.orglett.5b01608
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New Class of Heterogeneous Helical Peptidomimetics

Abstract: A new class of unnatural heterogeneous foldamers is reported to contain alternative α-amino acid and sulfono-γ-AA amino acid residues in a 1:1 repeat pattern. Two-dimensional NMR data show that two 1:1 α/sulfono-γ-AA peptides with diverse side chains form analogous right-handed helical structures in solution. The effects of sequence length, side chain, N-capping, and temperature on folding propensity were further investigated using circular dichroism and small-angle X-ray scattering.

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Cited by 26 publications
(43 citation statements)
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“…18b Gratifyingly, the reactions took place very efficiently without acetic anhydride capping after every coupling cycle, and ultimately the desired L-amino acid/D-sulfono- γ -AApeptide hybrids were obtained with decent yield after HPLC purification.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…18b Gratifyingly, the reactions took place very efficiently without acetic anhydride capping after every coupling cycle, and ultimately the desired L-amino acid/D-sulfono- γ -AApeptide hybrids were obtained with decent yield after HPLC purification.…”
Section: Resultsmentioning
confidence: 99%
“…Hitherto, all of the AApeptides were derived from natural L-amino acids, and we thus ended up with L-AApeptides. The folding propensity of oligomers bearing a L-sulfono- γ -AApeptide backbone has been investigated in solution by 2D-NMR studies, 18 which suggests homogeneous L-sulfono- γ -AApeptides and 1:1 α /L-sulfono- γ -AA hybrid peptides adopt helical conformations. However, it remains yet unknown the impact of the corresponding D-enantiomers of L- γ -AApeptide on the formation of helical secondary structures.…”
Section: Introductionmentioning
confidence: 99%
“…In addition, their antimicrobial mechanisms will be carried out more systematically, which could gain insight into the general mechanism of action in this class of peptidomimetics, so as to assess their potential to induce drug resistance in bacteria. Moreover, it would be very helpful if crystal structures [49,55] of certain antimicrobial γ-AApeptides can be obtained, which will assist in understanding their structure-function relationship and thus contributing to the future rational design. In addition, it is also critical to investigate the in vivo activity of antimicrobial γ-AApeptides, so as to better determine future science group No writing assistance was utilized in the production of this manuscript.…”
Section: Future Perspectivementioning
confidence: 99%
“…Peptidomimetics are designed to overcome the barriers posed by natural peptides such as premature proteolysis, low availability and less receptor selectivity 15 . This process of designing is initiated by forging structure-activity relationships (SAR) which tell about a minimal active sequence or the chief pharmacophore elements; also they recognize those essential residues responsible for a biological effect.…”
mentioning
confidence: 99%