Synthetic vaccines, consisting of subunits of pathogens, have the potential to address several challenges of conventional vaccines (live-attenuated or killed pathogens) such as instability, risk of infection, autoimmunity and manufacturing difficulties. However, synthetic vaccines have significant limitations including poor immunogenicity and fast degradation, necessitating co-administration with effective adjuvants and use of appropriate delivery systems. Current choices of effective and safe adjuvants and delivery systems are very limited, and formulations/conjugations of synthetic vaccines often do not lead to clinical success. Rational design and novel synthetic methods are in high demand to overcome obstacles in synthetic vaccine development. In this PhD research project, new antigen delivery platforms (lipopeptide-carbohydrate-antigen platforms) were developed by integrating a lipopeptide and a topology-controlling template to present and deliver synthetic antigens, which may serve as a generic strategy to develop safe and effective synthetic vaccines. The focus of this research was on the rational design and optimized chemical synthesis of the platforms. The design of the lipopeptide-carbohydrate-antigen platforms was inspired by the principle of self-adjuvanting lipopeptide vaccines that feature the covalent attachment of bacterial or synthetic lipids to peptide antigens. Lipopeptide vaccines have generally shown a good safety profile in human clinical trials and seen as a potential approach for human vaccination. The lipopeptide [C12-G-C12-C12-G; G: glycine; C12: 2-(R/S)-aminododecanoic acid] used in this study was derived from the lipid core peptide (LCP) system which has demonstrated high delivery capacity and synthetic flexibility in numerous applications. Aiming to introduce the topology-controlling feature to self-adjuvanting lipopeptide vaccines, this study introduced topological templates (carbohydrates) to the platforms, based on the concept of template assembled synthetic peptide (TASP) that has emerged as a de novo strategy to assemble peptides in a desired conformation. Five carbohydrate templates that varied in conformation and spacer were used in the platform design, providing an opportunity to optimize the antigen’s spatial arrangement. The ultimate aim of this research is to develop antigen delivery platforms which can be used for human vaccines. Therefore, optimized methods for the synthesis of the platforms were developed to achieve high purity and good yield of the final products. Two series of carbohydrate templates were first synthesized, with functional groups suitable for covalent conjugation to the lipopeptide moiety and multiple peptide antigens. The spatial conjugation positions and the length of the spacers of these templates were varied through modifications to the hydroxyl groups of glucose, galactose and mannose. To achieve an efficient conjugation of the sugar molecules and the peptides (lipopeptide and peptide antigens), techniques that were examined included solid phase peptide synthesis (SPPS) and native chemical ligation (NCL). The attempts using SPPS did not yield the target product when incorporating a model antigen (20-mer peptide epitope 8830; DNGKAIYERARERALQELGP; derived from group A streptococcal M protein) to a glucose-based template because of significant difficulties including low coupling efficiency and unsuccessful purification. In contrast, a series of lipopeptide-carbohydrate-8830 products were synthesized in high purity and good yield using NCL, after the solubility problem had been solved. The poor water solubility of the lipopeptide-carbohydrate constructs was significantly improved through co-lyophilization of the compounds with 1% (w/v) sodium dodecyl sulphate. Conformational studies of the synthesized vaccine candidates containing 8830 were performed using circular dichroism (CD). The data revealed that the attached antigenic peptides formed α-helix bundles in all cases. The result is in line with the common α-helix-inducing feature of carbohydrate templates. This approach was extended to incorporate synthetic J14i (14-mer peptide epitope; ASREAKKQVEKALE; derived from group A streptococcal M protein) in an effort to induce its α-helicity. Embedding this minimal epitope in helix-promoting peptide sequences was previously developed in literature to mimic J14i’s helical structure at the corresponding site of the native protein. However, the introduction of “foreign” peptide sequences is believed to have an unfavourable impact on the antigen specificity. This work employed a non-peptide approach, using the developed topological carbohydrate templates, to induce helical conformation of the peptide antigen. CD studies confirmed that the template-assembled peptide J14i formed α-helix bundles. This strategy also reduces the complexity and cost of vaccine production by simply reducing the peptide size. Preliminary immunological evaluation demonstrated antigen-specific immune responses elicited by the synthesized vaccine candidates containing 8830, with vaccines based on different carbohydrate templates exhibiting varied efficacy. This data suggested that the different spatial structure of the vaccine candidates had key influence on the vaccine efficacy, pointing out the future direction of customizing carbohydrate templates for specific antigens.