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Abstract
This paper describes the synthesis of peptide fragments for use in a new type of combinatorial discovery technology, in which the building blocks are brought together by non-covalent interactions, rather than direct chemical bonding. The building blocks of interest—in this case different amino acids—are converted to amphiphiles by attachment to lipid tails. The amphiphiles, when mixed together in aqueous phase, are designed so that they aggregate spontaneously to form micelles. The building blocks form the headgroups of each of the amphiphiles, and these headgroups cover the surface of the micelle in a dynamic close-packed fluid mosaic array. These building blocks come together so closely that two- or three-dimensional structures are created on the surface of the micelles, and these can be screened in biological assays to find out which combination of building blocks is able to elicit a biological response. Lipopeptides consisting of two residues of lipoamino acid and other amino acids moieties have been designed, synthesized, characterized and the ability of these constructs to form supra-molecular assemblies is demonstrated.
Highlights
Conventional methods of drug discovery often employ combinatorial chemistry as part of the methodology to create new structures as potential ligands for binding to biological targets [1,2,3,4]
This paper describes the synthesis of peptide fragments for use in a new type of combinatorial discovery technology, in which the building blocks are brought together by non-covalent interactions, rather than direct chemical bonding
Lipopeptides consisting of two residues of lipoamino acid and other amino acids moieties have been designed, synthesized, characterized and the ability of these constructs to form supra-molecular assemblies is demonstrated
Summary
Conventional methods of drug discovery often employ combinatorial chemistry as part of the methodology to create new structures as potential ligands for binding to biological targets [1,2,3,4]. The need for chemical linkages introduces physical constraints on the molecules under study They are usually linear, and do not have free rotation about the bonds which joining them together so that even if the right combination of building blocks is selected, it is possible that they will not have the right orientation with respect to each other to interact appropriately with the target. For these reasons, we have devised a combinatorial screening system in which amino-acid building blocks are brought together without the use of covalent linkages. Amino acids, usually glycine and serine, are used a spacers between the lipid tail and headgroup
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