Human cathelicidin antimicrobial peptide (CAMP/LL-37) is a cationic antimicrobial peptide that is widely expressed by myeloid and epithelial cells at the human-environment interface. It possesses broad spectrum antimicrobial capacity against bacteria, fungi and viruses. In addition to its direct antimicrobial activity, CAMP/LL-37 also attracts and recruits monocytes, neutrophils and other...
The human cathelicidin antimicrobial peptide (CAMP) is a broad spectrum microbicidal agent and modulator of both the innate and adaptive immune system. It is induced by 1,25-dihydroxyvitamin D (1,25(OH)₂D₃) through activation of the vitamin D receptor (VDR) and primary bile salts through activation of the xenobiotic nuclear receptor farnesoid X...
In this dissertation I study evolutionary patterns at genes encoding antimicrobial peptides (AMPs) in frogs. AMPs are short, amphipathic, cationic, secreted proteins that kill bacteria and other pathogens through a non-catalytic mechanism that involves
binding to and disrupting the microbial cell membrane. In many animal taxa, positive selection is much...
This thesis describes the chemical investigation of marine cyanobacteria collected in Madagascar and Panama with an emphasis on the isolation and structure elucidation of medicinally relevant secondary metabolites.
A collection of the marine cyanobacterium Lyngbya majuscula from the Radames Islands, Madagascar yielded two new cyclic depsipeptides, radamamides A and B,...
The adsorption and elution of the antimicrobial peptide nisin at hydrophobic,
silanized silica surfaces coated with the poly[ethylene oxide]-poly[propylene oxide]-
poly[ethylene oxide] surfactant Pluronic® F108 was measured in situ, with ellipsometry.
While such layers are known to inhibit protein adsorption, nisin was observed to adsorb in
multilayer quantities, to an...