Inhibition of complement activation, myeloperoxidase, NET formation and oxidant activity by PIC1 peptide variants.

ABSTRACT:

Background

A product of rational molecular design, PA-dPEG24 is the lead derivative of the PIC1 family of peptides with multiple functional abilities including classical complement pathway inhibition, myeloperoxidase inhibition, NET inhibition and antioxidant activity. PA-dPEG24 is composed of a sequence of 15 amino acid, IALILEPICCQERAA, and contains a monodisperse 24-mer PEGylated moiety at its C terminus to increase aqueous solubility. Here we explore a sarcosine substitution scan of the PA peptide to evaluate impacts on solubility in the absence of PEGylation and functional characteristics.

Methods

Sixteen sarcosine substitution variants were synthesized and evaluated for solubility in water. Aqueous soluble variants were then tested in standard complement, myeloperoxida

SUBMITTER: Hair PS 

PROVIDER: S-EPMC6938345 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature