Immunotherapy for Pulmonary TB
AMPs are small cationic molecules of a variable length. These peptides mainly constitute polar-hydrophilic, nonpolar-hydrophobic and positively charged amino acids. This special conformation gives the molecule amphipathic and cationic properties, which are very important for their bactericidal activity. AMPs are broadly distributed in nature and all of them share fundamental structural characteristics that are very important for their broad-spectrum antimicrobial activity, such as length (less than 60 amino acids), amphipathic structure and the presence of cationic amino acids in their structure, providing them with a partial positive charge. However, due to their secondary structural characteristics, AMPs could be divided into subcategories that include: α-helical, peptides enriched with repetition of one amino acid, and peptides with intramolecular bonding formed by cysteines. These features allow the AMPs to interact with most microorganisms' lipid bilayer and eliminate them through membrane disruption or by translocating across the membrane and inhibiting cytosolic targets.
Recent findings show that the immunoregulatory activity is quite efficient since most of these activities have an effect at the nanomolar scale, acting over several innate immune response receptors. Although at the beginning it was thought that these functions were only focused to promote proinflammatory conditions, it is now well known that some peptides, such as cathelicidin have ambiguous functions promoting, in certain cases, an anti-inflammatory response as well.
Basic Facts
AMPs are small cationic molecules of a variable length. These peptides mainly constitute polar-hydrophilic, nonpolar-hydrophobic and positively charged amino acids. This special conformation gives the molecule amphipathic and cationic properties, which are very important for their bactericidal activity. AMPs are broadly distributed in nature and all of them share fundamental structural characteristics that are very important for their broad-spectrum antimicrobial activity, such as length (less than 60 amino acids), amphipathic structure and the presence of cationic amino acids in their structure, providing them with a partial positive charge. However, due to their secondary structural characteristics, AMPs could be divided into subcategories that include: α-helical, peptides enriched with repetition of one amino acid, and peptides with intramolecular bonding formed by cysteines. These features allow the AMPs to interact with most microorganisms' lipid bilayer and eliminate them through membrane disruption or by translocating across the membrane and inhibiting cytosolic targets.
Recent findings show that the immunoregulatory activity is quite efficient since most of these activities have an effect at the nanomolar scale, acting over several innate immune response receptors. Although at the beginning it was thought that these functions were only focused to promote proinflammatory conditions, it is now well known that some peptides, such as cathelicidin have ambiguous functions promoting, in certain cases, an anti-inflammatory response as well.
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