The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Peptidomimetics via modifications of amino acids and peptide bonds
Abstract
Peptidomimetics represent an important field in chemistry, pharmacology and material science as they circumvent the limitations of traditional peptides used in therapy. Self-structural organizations such as turns, helices, sheets and loops can be accessed by chemical modifications of amino acids or peptides. In-depth structural and conformational analysis and structure-activity relationships (SAR) offer a way to establish peptidomimetic libraries. Herein, we review recent developments in peptidomimetics that are formed via heteroatom replacement within the native amino acid backbone. Each sub-section describes structural features, utility and preparative methods.
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Cites
Contemporary strategies for peptide macrocyclization
White, C. J., & Yudin, A. K. (2011) · Nature Chemistry · doi:10.1038/nchem.1062 · Cited by 1,088
Lien, S., & Lowman, H. B. (2003) · Trends in Biotechnology · doi:10.1016/j.tibtech.2003.10.005 · Cited by 209
Cited by
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Agouridas, V., El Mahdi, O., Diemer, V., Cargoët, M., Monbaliu, J.-C. M., & Melnyk, O. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00712 · Cited by 650
Palomo, J. M. (2014) · RSC Adv. · doi:10.1039/c4ra02458c · Cited by 273
Rajasekhar, K., & Govindaraju, T. (2018) · RSC Advances · doi:10.1039/c8ra03620a · Cited by 150
Protease-Resistant Peptides for Targeting and Intracellular Delivery of Therapeutics
Lucana, M. C., Arruga, Y., Petrachi, E., Roig, A., Lucchi, R., & Oller-Salvia, B. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13122065 · Cited by 102
Metadata
- Authors
- Avan, I., Hall, C. D., & Katritzky, A. R.
- Venue
- Chemical Society Reviews
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2014
- Volume
- 43
- Issue
- 10
- Pages
- 3575
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- OpenAlex
- W1964580701
- Cited by
- 283
- References
- 2
- FWCI
- 1.37
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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