All Outputs (3)

Expedient synthesis of a novel class of pseudoaromatic amino acids: Tetrahydroindazol-3-yl- and tetrahydrobenzisoxazol-3-ylalanine derivatives (2003)
Journal Article
Middleton, R. J., Mellor, S. L., Chhabra, S. R., Bycroft, B. W., & Chan, W. C. (2004). Expedient synthesis of a novel class of pseudoaromatic amino acids: Tetrahydroindazol-3-yl- and tetrahydrobenzisoxazol-3-ylalanine derivatives. Tetrahedron Letters, 45(6), 1237-1242. https://doi.org/10.1016/j.tetlet.2003.11.133

A concise synthesis of novel homochiral aromatic amino acid surrogates comprising a tetrahydroindazole or a benzisoxazole system was developed via the acylation of a cyclic 1,3-diketone by the side-chain carboxyl functionality of either Boc-Asp-OtBu... Read More about Expedient synthesis of a novel class of pseudoaromatic amino acids: Tetrahydroindazol-3-yl- and tetrahydrobenzisoxazol-3-ylalanine derivatives.

Side-chain-to-tail thiolactone peptide inhibitors of the staphylococcal quorum-sensing system (2003)
Journal Article
Scott, R. J., Lian, L. Y., Muharram, S. H., Cockayne, A., Wood, S. J., Bycroft, B. W., …Chan, W. C. (2003). Side-chain-to-tail thiolactone peptide inhibitors of the staphylococcal quorum-sensing system. Bioorganic and Medicinal Chemistry Letters, 13(15), 2449-2453. https://doi.org/10.1016/S0960-894X%2803%2900497-9

The expression of many staphylococcal virulence factors are regulated by the agr locus via a two-component signal transduction system (TCSTS), which is activated in response to a secreted autoinducer peptide (AIP). By exploiting the unique chemical a... Read More about Side-chain-to-tail thiolactone peptide inhibitors of the staphylococcal quorum-sensing system.

Liposome entrapment and immunogenic studies of a synthetic lipophilic multiple antigenic peptide bearing VP1 and VP3 domains of the hepatitis A virus: A robust method for vaccine design (2003)
Journal Article
Haro, I., Pérez, S., García, M., Chan, W. C., & Ercilla, G. (2003). Liposome entrapment and immunogenic studies of a synthetic lipophilic multiple antigenic peptide bearing VP1 and VP3 domains of the hepatitis A virus: A robust method for vaccine design. FEBS Letters, 540(1-3), 133-140. https://doi.org/10.1016/S0014-5793%2803%2900249-7

Multiple antigen peptides (MAP) have been demonstrated to be efficient immunological reagents for the induction of immune responses to a variety of infectious agents. Several peptide domains of the hepatitis A virus (HAV) capsid proteins, mainly VP1... Read More about Liposome entrapment and immunogenic studies of a synthetic lipophilic multiple antigenic peptide bearing VP1 and VP3 domains of the hepatitis A virus: A robust method for vaccine design.