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Lipopeptides activate the immune system through receptors.

Lipopeptides containing lipid-core peptides linking synthetic analogs of Pam3Cys to multiple peptides via dendrimeric multiple antigen peptide structures have proven to be effective for Group A streptococcal (GAS) vaccines. Lipopeptides are biological molecules that consist of lipid groups connected to peptide moieties. Many bacteria express these types of molecules.

Lipopeptides are recognized by toll like receptors such as TLR1. Short peptide sequences including small lipopeptides or peptide epitopes that contain lipopeptides play a major role in immune recognition. A pathogen, such as bacteria or a parasite, is captured when encountered and degraded by specialized antigen presenting cells of the immune system into short peptide sequences known as epitopes. These epitopes are then presented to effector T cells and, if the correct cellular signals are given, can trigger off a cascade of events that eventually induces an immune response.

Synthetic lipopeptides have been used for the design of vaccines in the past. If the epitope that is recognized by an antibody or a T cell is known, a vaccine can be designed around this epitope. Lipopeptide such as Macrophage Activating LipoPeptide-2 (MALP-2) can be used to deliver antigenic peptides that contain toll like receptor (TLR) agonists. MALP-2 is a diacylated lipopeptide originally isolated from Mycoplasma Fermentans which is recognized by TLR6 only when heterodimerized with TLR2. The CD36 protein is a member of the scavenger receptor type B family and acts as a facilitator or co-receptor for MALP-2 recognition through the TLR2/TLR6 complex.


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