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Rose's Project Page - RISE summer 2004 |
Intern: Rose Nguyen, UCSB
Mentor: Alex Chu-Kung
Faculty Supervisor: Matthew Tirrell
Department: Chemical Engineering |
EFFECTS OF SELF-ASSEMBLY ON PEPTIDE ANTIMICROBIAL ACTIVITY
It has been found that some naturally occurring peptides are bactericidal
towards a broad spectrum of bacteria, including many drug resistant strains.
These antimicrobial peptides operate by a novel mechanism, the permeabilization
of bacterial cell membranes. As a result, it is difficult for bacteria to
develop resistance towards these peptides since resistance would require
restructuring its cell wall. To do this the cell must evolve drastically,
which is highly unlikely. One strategy used to affect peptide properties is
conjugation of the peptide to saturated hydrocarbon chains. Doing this changes
various properties of the peptide including hydrophobicity and creates an
amphiphilic peptide conjugate, called a peptide amphiphile. Peptide amphiphiles
with lipid-like tails have been shown to form vesicles. Peptide functionalized
vesicles allow us to study the effect of peptide orientation and assembly on
antimicrobial activity. By modifying various factors, such as size, shape, and
composition, a relationship between the effects of solution self-assembly of
peptides and their relationship to antimicrobial activity can be achieved.
Antimicrobial peptides are being considered as a drug candidate for the future.
This can open new doors on how drugs are made, and possibly create a new form
of drug delivery.
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