The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Alpha-helical antimicrobial peptides—Using a sequence template to guide structure–activity relationship studies
Open accessAbstract
An important class of cytolytic antimicrobial peptides (AMPs) assumes an amphipathic, alpha-helical conformation that permits efficient interaction with biological membranes. Host defence peptides of this type are widespread in nature, and numerous synthetic model AMPs have been derived from these or designed de novo based on their characteristics. In this review we provide an overview of the 'sequence template' approach which we have used to design potent artificial helical AMPs, to guide structure-activity relationship studies aimed at their optimization, and to help identify novel natural AMP sequences. Combining this approach with the rational use of natural and non-proteinogenic amino acid building blocks has allowed us to probe the individual effects on the peptides' activity of structural and physico-chemical parameters such as the size, propensity for helical structuring, amphipathic hydrophobicity, cationicity, and hydrophobic or polar sector characteristics. These studies furthermore provided useful insights into alternative modes of action for natural membrane-active helical peptides.
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Cites
Antimicrobial peptides of multicellular organisms
Zasloff, M. (2002) · Nature · doi:10.1038/415389a · Cited by 8,457
Tödtling, F., & Trippl, M. (2005) · Research Policy · doi:10.1016/j.respol.2005.01.018 · Cited by 2,571
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Metadata
- Authors
- Zelezetsky, I., & Tossi, A.
- Venue
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Publisher
- Elsevier BV
- Published
- 2006-09
- Volume
- 1758
- Issue
- 9
- Pages
- 1436-1449
- ISSN
- 0005-2736 (ISSN-L)
- OpenAlex
- W2170912840
- Cited by
- 439
- References
- 2
- FWCI
- 11.25
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Zelezetsky, I., & Tossi, A. (2006). Alpha-helical antimicrobial peptides—Using a sequence template to guide structure–activity relationship studies. Biochimica et Biophysica Acta (BBA) - Biomembranes. https://doi.org/10.1016/j.bbamem.2006.03.021
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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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