33 research outputs found
Restored invasion of mouse MO4 cells into chick heart in vitro through mutual conditioning at reduced temperature.
Effect of lipid-derivatives on invasion in vitro and on surface glycoproteins of three rodent cell types.
A
Decreased fucose incorporation in cell surface carbohydrates is associated with inhibition of invasion.
A heterodimer comprised of two bovine lactoferrin antimicrobial peptides exhibits powerful bactericidal activity against Burkholderia pseudomallei
Effect of racemic 1-o-octadecyl-2-o-methylglycero-3-phosphocholine (ET-18-OCH3) on invasion in vitro and on N-linked surface glycosylation
C
Membrane-active mechanism of LFchimera against Burkholderia pseudomallei and Burkholderia thailandensis
Evaluation of salivary mucins in children with deciduous and mixed dentition: comparative analysis between high and low caries-risk groups
Cyclizing disulfide-rich peptides using sortase A
Sortase A (SrtA) is an enzyme obtained from Staphylococcus aureus that catalyzes site-specific transpeptidation of surface proteins to the bacterial cell membrane. SrtA recognizes an LPXTG amino acid motif and cleaves between the Thr and Gly to form a thioester-linked acyl–enzyme intermediate. The intermediate is resolved in the presence of a nucleophilic N-terminal polyglycine resulting in ligation of the acyl donor to the polyglycine acceptor. Here we describe the application of SrtA as a tool for the cyclization of disulfide-rich peptides. Reactions are typically tailored to each disulfide-rich peptide with optimal conditions producing yields of 40–50% cyclized peptide