Interleukin-8 antagonists generated by N-terminal modification.

Antagonists of monocyte chemoattractant protein 1 identified by modification of functionally critical NH2-terminal residues

Monocyte chemoattractant protein (MCP)-1 analogues were designed to determine the role of the NH2-terminal region in structure and function. The NH2-terminal residue was important for function and receptor binding, as it could not be deleted or extended. However the NH2-terminal pyroglutamate residue of the wild type was not essential as it could be replaced by several other noncyclic amino aci...

Interleukin Antagonists

There is strong experimental and clinical support for a causal role of immune dysregulation and inflammation in atherosclerosis and heart failure. Atherosclerotic lesions are infiltrated by monocytes, macrophages, and T lymphocytes (predominantly Th1). Cytokines, including interleukin-6 (IL6) and tumor necrosis factor-α (TNF-α), are released by the infiltrating inflammatory cells and stimulate ...

Mapping the binding surface of interleukin-8 complexed with an N-terminal fragment of the type 1 human interleukin-8 receptor.

Interleukin-8 and its receptors are key mediators of immune and inflammatory responses. Heteronuclear NMR spectroscopy has been utilized to map the binding surface on interleukin-8 (IL-8) for an N-terminal fragment of the human Type-1 IL-8 receptor. A peptide corresponding to residues 1-40 of the IL-8 type 1 receptor (IL8-r1) was titrated into a sample of uniformly 15N-labeled IL-8. IL8-r1 bind...

N-Terminal Modification of Proteins with o-Aminophenols

The synthetic modification of proteins plays an important role in chemical biology and biomaterials science. These fields provide a constant need for chemical tools that can introduce new functionality in specific locations on protein surfaces. In this work, an oxidative strategy is demonstrated for the efficient modification of N-terminal residues on peptides and N-terminal proline residues on...

N-terminal protein modification through a biomimetic transamination reaction.