Date Approved

2012

Degree Type

Open Access Thesis

Degree Name

Master of Science (MS)

Department or School

Chemistry

Committee Member

Deborah Heyl-Clegg, PhD

Comments

The increasingly growing resistance to antibiotics has geared research efforts towards understanding the structure and function of antimicrobial peptides to gradually replace or reinforce the roles of antibiotics in therapeutic applications. Cathelicidins are a family of structurally diverse antimicrobial peptides that have only a single representative in humans, an antimicrobial peptide called LL37. LL37 is believed to play an important role in the first line of defense against local infection and systemic invasion of pathogens at sites of inflammation and wounds. LL37 kills bacteria by disrupting their membranes through non-specific peptide-lipid interactions, making it far more difficult for bacteria to develop resistance against than current antibacterial agents. Examining analogs of LL37 could provide insight into its structure, function, and antimicrobial properties. Three of these variations were synthesized and purified: two truncated forms of LL37 (SK29 and FF33) as well as N-terminally extended LL37 (FALL39) for comparative studies.

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