Open Access Honors Program Thesis
ln KW ALP23 peptides containing Lysine and Trp, as the Trps were moved further in towards the center of the bilayer, Lys became the dominant anchoring residue (1). The goal of this project was to determine whether Arg exhibits snorkeling behavior similar to Lys, and is able to anchor the peptide in the membrane despite the repositioning of Trp in the RWALP peptides. Several candidate R W ALP23 peptides containing Tryptophan and Arginine with an alternating LeucineAlanine backbone were synthesized successfully. They were then studied by HPLC, CD, and MALDI-TOF Mass Spectrometry to investigate the anchoring roles of Arg and Trp. The CD spectra showed a decreasing trend in alpha-helical conformation as the Trps were moved closer to the bilayer center, suggesting that Arg anchors the peptide to the membrane better with the assistance of Trp.
Year of Submission
Department of Chemistry and Biochemistry
University Honors Designation
A thesis submitted in partial fulfillment of the requirements for the designation University Honors
1 PDF file (19 pages)
©2005 Eugenia Christine Tsamis
Tsamis, Eugenia Christine, "Synthesis and Characterization of Membrane Anchored Peptides" (2005). Honors Program Theses. 616.