Neuropeptides are essential to neuron function and significantly affect behavioral response. While neuropeptides are beneficial for behavior, at high concentrations they can be detrimental to cell function. Recent research shows that amino acid substitutions in neuropeptides could lead to changes in the cell entering mechanisms. We investigated the structure-function of modified neuropeptides families of FaRP (FLP-3-2 and FLP-3-9) and TRH (TRH-1A and TRH-1B) using dielectric relaxation spectroscopy (DRS) and circular dichroism (CD). We measured the complex dielectric permittivity and conductivity of the neuropeptides in the frequency range 200mHz to 40MHz at 0.5μM and 1μM. We determined the structure of the neuropeptides using CD data and compared it to computational models. We found that the longer amino acids chain neuropeptide FLP-3-9 has a lower permittivity than FLP-3-2. A decrease in permittivity was also observed when the Arginine and Glycine were substituted with Asparagine and Alanine in TRH. Knowing the complete structure and function of modified neuropeptides leads to further complex sequencing of TRH and FLP in neurobiology.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Lunden, Benjamin
• Hershoff, Allison

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-050222-153020
• 67146

Advisor

• Srinivasan, Jagan
• Stroe, Izabela RC

Year

• 2022

Date created

• 2022-05-02

Resource type

• Major Qualifying Project

Major

• Physics

Rights statement

• In Copyright