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α-Calcitonin gene related peptide (αCGRP) inhibitors are important medicinal targets due to their ability to produce antimigraine effects, thus, the discovery of long-acting αCGRP inhibitors is of significant interest. Herein we report the synthesis of an isotopically labelled version of the well-known CGRP receptor antagonist, αCGRP8-37 , as well as lipidated αCGRP8-37 with comparable antagonistic activity. These isotopically labelled peptides can be employed in assays to determine the metabolic stability of the lipidated αCGRP8-37 and compare this with the stability of known αCGRP8-37 .

Agonists of Toll-like Receptor 2 (TLR2) are attractive synthetic targets due to their use as adjuvants in immunotherapies to treat various diseases notably, cancer. An indepth understanding of TLR2 agonist structure-activity relationships is therefore advantageous for the methodical design of vaccines targetting the TLR2 machinery. This review aims to collate and discuss the literature regarding synthetic studies towards TLR2 agonists and the structure-activity relationships thereof. It is hoped that interested readers will gain a holistic understanding of this topic, and will prompt further efforts towards finding effective agonists of TLR2.

α-Calcitonin gene related peptide (αCGRP) inhibitors are important medicinal targets due to their ability to produce antimigraine effects, thus, the discovery of long-acting αCGRP inhibitors is of significant interest. Herein we report the synthesis of an isotopically labelled version of the well-known CGRP receptor antagonist, αCGRP

Cancer immunotherapy has gained increasing attention due to its potential specificity and lack of adverse side effects when compared to more traditional modes of treatment. Toll-like receptor 2 (TLR2) agonists are lipopeptides possessing the S-[2,3-bis(palmitoyloxy)propyl]-l-cysteine (Pam2Cys) motif and exhibit potent immunostimulatory effects. These agonists offer a means of providing "danger signals" in order to activate the immune system toward tumor antigens. Thus, the development of TLR2 agonists is attractive in the search of potential immunostimulants for cancer. Existing SAR studies of Pam2Cys with TLR2 indicate that the structural requirements for activity are, for the most part, very intolerable. We have investigated the importance of stereochemistry, the effect of N-terminal acylation, and homologation between the two ester functionalities in Pam2Cys-conjugated lipopeptides on TLR2 activity. The R diastereomer is significantly more potent than the S diastereomer and N-terminal modification generally lowers TLR2 activity. Most notably, homologation gives rise to analogues which are comparatively active to the native Pam2Cys containing constructs.