Study of a Model α-Helix Peptide’s Surface Properties by Langmuir Monolayer Techniques and Surface FTIR

dc.contributor.advisor Wang, Chengshan Combs, Joseph Dale
dc.contributor.committeemember Chong, Ngee
dc.contributor.committeemember Bicker, Kevin
dc.contributor.department Chemistry en_US 2016-08-15T15:06:31Z 2016-08-15T15:06:31Z 2016-06-24
dc.description.abstract Cell membranes have been shown to be able to change the conformation of proteins/peptides. However, the structure of the cell membrane is complicated and has been divided to three regions: the hydrophobic region containing alkyl chains, the hydrophilic head group, and the hydration layer, or lipid-water interface, which exists between the hydrophilic head group and the bulk water solution, but with lower dielectric constant compared with fully hydrated water. The air-water interface has been used to mimic the structure of the hydration layer because of their similar dielectric constant.1,2 Some proteins were found to form a stable Langmuir monolayer and accumulate at the air-water interface. For example, α-synclein, a membrane protein containing 140 amino acids, is unstructured in aqueous solution but changes its conformation to α-helix at the air-water interface. This incites interest to investigate short motifs of α-helix to form a stable Langmuir monolayer at the air-water interface. In this thesis, a peptide with sequence of YAAAA(KAAAA)4 (referred as Pep25 hereafter) was used as a model peptide of α-helix to spread at the air-water interface, because our group has determined the conformation of Pep25 in residue level by the 13C isotope-edited FTIR. Langmuir monolayer technique together with IRRAS showed that Pep25 does not form a typical Langmuir monolayer at the interface. Potential plans to make Pep25 to form a stable monolayer are also discussed in this thesis. M.S.
dc.publisher Middle Tennessee State University
dc.subject Air-water
dc.subject Interface
dc.subject Langmuir Monolayer
dc.subject Model membrane
dc.subject Model Peptide
dc.subject Peptide
dc.subject.umi Chemistry
dc.subject.umi Biochemistry
dc.subject.umi Analytical chemistry
dc.thesis.degreegrantor Middle Tennessee State University
dc.thesis.degreelevel Masters
dc.title Study of a Model α-Helix Peptide’s Surface Properties by Langmuir Monolayer Techniques and Surface FTIR
dc.type Thesis
Original bundle
Now showing 1 - 1 of 1
No Thumbnail Available
5.69 MB
Adobe Portable Document Format