C-H activation: Complex peptides made simple.
Naturally occurring peptides exhibit an extraordinary range of properties and biological activities1. Nonribosomal peptides (NRPs) continue to represent an invaluable source of new small-molecule drugs2, having already provided antibiotics such as the β-lactam, glycopeptide and lipopeptide families3...
| Main Authors: | , |
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| Format: | Journal article |
| Language: | English |
| Published: |
Nature Publishing Group
2017
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| _version_ | 1797073220743987200 |
|---|---|
| author | Bartlett, S Spring, DR |
| author_facet | Bartlett, S Spring, DR |
| author_sort | Bartlett, S |
| collection | OXFORD |
| description | Naturally occurring peptides exhibit an extraordinary range of properties and biological activities1. Nonribosomal peptides (NRPs) continue to represent an invaluable source of new small-molecule drugs2, having already provided antibiotics such as the β-lactam, glycopeptide and lipopeptide families3. Advances in the bioengineering of NRP synthases4 and the availability of non‑proteinogenic amino acids have expanded the compound pool available to researchers in recent years, but chemical synthesis remains the tool of choice for the study of structural modifications on NRP derivatives nonetheless. Analogue synthesis is particularly laborious for structurally complex peptides when each one must be made from the ground up. |
| first_indexed | 2024-03-06T23:18:59Z |
| format | Journal article |
| id | oxford-uuid:681a7c0a-325b-4375-9e4e-7b8d9c36d306 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:18:59Z |
| publishDate | 2017 |
| publisher | Nature Publishing Group |
| record_format | dspace |
| spelling | oxford-uuid:681a7c0a-325b-4375-9e4e-7b8d9c36d3062022-03-26T18:42:38ZC-H activation: Complex peptides made simple.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:681a7c0a-325b-4375-9e4e-7b8d9c36d306EnglishSymplectic Elements at OxfordNature Publishing Group2017Bartlett, SSpring, DRNaturally occurring peptides exhibit an extraordinary range of properties and biological activities1. Nonribosomal peptides (NRPs) continue to represent an invaluable source of new small-molecule drugs2, having already provided antibiotics such as the β-lactam, glycopeptide and lipopeptide families3. Advances in the bioengineering of NRP synthases4 and the availability of non‑proteinogenic amino acids have expanded the compound pool available to researchers in recent years, but chemical synthesis remains the tool of choice for the study of structural modifications on NRP derivatives nonetheless. Analogue synthesis is particularly laborious for structurally complex peptides when each one must be made from the ground up. |
| spellingShingle | Bartlett, S Spring, DR C-H activation: Complex peptides made simple. |
| title | C-H activation: Complex peptides made simple. |
| title_full | C-H activation: Complex peptides made simple. |
| title_fullStr | C-H activation: Complex peptides made simple. |
| title_full_unstemmed | C-H activation: Complex peptides made simple. |
| title_short | C-H activation: Complex peptides made simple. |
| title_sort | c h activation complex peptides made simple |
| work_keys_str_mv | AT bartletts chactivationcomplexpeptidesmadesimple AT springdr chactivationcomplexpeptidesmadesimple |