Date of Publication

8-2025

Document Type

Bachelor's Thesis

Degree Name

Bachelor of Science in Biochemistry

Subject Categories

Biochemistry, Biophysics, and Structural Biology

College

College of Science

Department/Unit

Chemistry

Thesis Advisor

Rafael A. Espiritu

Defense Panel Member

Raymond S. Malabed
Searle Aichelle S. Duay

Abstract/Summary

Antimicrobial resistance (AMR) represents one of the most pressing public health challenges of the 21st century. Antimicrobial peptides (AMPs) offer a promising alternative to traditional antibiotics due to their broad-spectrum efficacy against a wide range of pathogens. This study investigates peptides derived from the transmembrane region of Gasdermin A3 (GSDMA3), a protein known for its role in pyroptosis. Both the wild-type (WGA3) and modified (MGA3) peptide sequences were evaluated for their interactions with multilamellar vesicles (MLVs) composed of (a) dipalmitoylphosphatidylethanolamine (DPPE), dipalmitoylphosphatidylglycerol (DPPG), and (b) dipalmitoylphosphatidylcholine (DPPC) powders, simulating the lipid bilayers of Gram-negative bacteria (3:1 DPPE/DPPG) and mammalian membranes (pure DPPC), respectively. Differential scanning calorimetry (DSC) was utilized to analyze the thermotropic phase behavior and membrane morphological changes of the lipid membrane mimics after peptide addition. The anionic WGA3 did not significantly alter either the bacterial or mammalian membrane models, suggesting its weak membrane-binding capacity. Similarly, the addition of MGA3 did not elicit significant changes in the mammalian and bacterial membrane models, with only minor shifts suggesting potential surface-level membrane interactions.

Abstract Format

html

Language

English

Format

Electronic

Keywords

Peptide antibiotics; Calorimetry

Upload Full Text

wf_yes

Embargo Period

8-18-2026

Download

Available for download on Tuesday, August 18, 2026

Share

COinS