Chemistry & Biology
Volume 17, Issue 9, 24 September 2010, Pages 970-980
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Article
Structural Studies of a Peptide with Immune Modulating and Direct Antimicrobial Activity

https://doi.org/10.1016/j.chembiol.2010.07.007Get rights and content
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Summary

The structure and function of the synthetic innate defense regulator peptide 1018 was investigated. This 12 residue synthetic peptide derived by substantial modification of the bovine cathelicidin bactenecin has enhanced innate immune regulatory and moderate direct antibacterial activities. The solution state NMR structure of 1018 in zwitterionic dodecyl phosphocholine (DPC) micelles indicated an α-helical conformation, while secondary structures, based on circular dichroism measurements, in anionic sodium dodecyl sulfate (SDS) and phospholipid vesicles (POPC/PG in a 1:1 molar ratio) and simulations revealed that 1018 can adopt a variety of folds, tailored to its different functions. The structural data are discussed in light of the ability of 1018 to potently induce chemokine responses, suppress the LPS-induced TNF-α response, and directly kill both Gram-positive and Gram-negative bacteria.

Highlights

► The structure and activity of the peptide IDR-1018 are presented ► The sequence of this peptide was derived using quantitative structure-activity relationship (QSAR) methodology ► 1018 displays both immunomodulatory and antimicrobial activities

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3

These authors contributed equally to this work