Add to ORKGABSTRACT: In a previous report we described the selection of potent, â-sheet pore-forming peptides from a combinatorial library designed to mimic membrane-spanning â-hairpins (Rausch, J. M., Marks, J. R.
β-hairpin antimicrobial peptides (AMPs) are small, usually cationic peptides that provide innate bio...
There are many opportunities to use macromolecules, such as peptides and oligonucleotides, for intra...
To better understand the sequence-structure-function relationships that control the activity and sel...
We recently developed an orthogonal, high-throughput assay to identify peptides that self-assemble i...
Abstract The use of designed antimicrobial peptides as drugs has been impeded by the ...
Abstract: Pore-forming peptides are of interest due to their antimicrobial activity and ability to f...
AbstractTo enable selection and characterization of highly potent pore-forming peptides, we develope...
Pore-forming proteins (PFPs) and small antimicrobial peptides (AMPs) represent a large family of mol...
Antimicrobial peptides have shown great potential as pharmaceutical agents, they are being considere...
Beta-sheets, in the form of the b-barrel folding motif, are found in several constitutive membrane p...
The mechanism of pore formation of lytic peptides, such as melittin from bee venom, is thought to in...
AbstractThe β-barrel and β-helix formation, as in porins and gramicidin, respectively, represent two...
It has previously been shown that an amphipathic de novo designed peptide made of 10 leucines and fo...
AbstractIn this work, we sought to rationally design membrane-active peptides that are triggered by ...
ABSTRACT: Antimicrobial peptides are known to form pores in cell membranes. We study this process in...
β-hairpin antimicrobial peptides (AMPs) are small, usually cationic peptides that provide innate bio...
There are many opportunities to use macromolecules, such as peptides and oligonucleotides, for intra...
To better understand the sequence-structure-function relationships that control the activity and sel...
We recently developed an orthogonal, high-throughput assay to identify peptides that self-assemble i...
Abstract The use of designed antimicrobial peptides as drugs has been impeded by the ...
Abstract: Pore-forming peptides are of interest due to their antimicrobial activity and ability to f...
AbstractTo enable selection and characterization of highly potent pore-forming peptides, we develope...
Pore-forming proteins (PFPs) and small antimicrobial peptides (AMPs) represent a large family of mol...
Antimicrobial peptides have shown great potential as pharmaceutical agents, they are being considere...
Beta-sheets, in the form of the b-barrel folding motif, are found in several constitutive membrane p...
The mechanism of pore formation of lytic peptides, such as melittin from bee venom, is thought to in...
AbstractThe β-barrel and β-helix formation, as in porins and gramicidin, respectively, represent two...
It has previously been shown that an amphipathic de novo designed peptide made of 10 leucines and fo...
AbstractIn this work, we sought to rationally design membrane-active peptides that are triggered by ...
ABSTRACT: Antimicrobial peptides are known to form pores in cell membranes. We study this process in...
β-hairpin antimicrobial peptides (AMPs) are small, usually cationic peptides that provide innate bio...
There are many opportunities to use macromolecules, such as peptides and oligonucleotides, for intra...
To better understand the sequence-structure-function relationships that control the activity and sel...