Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/42969
Title: STRUCTURAL STUDIES OF THE HUMAN ANTIMICROBIAL PEPTIDE DERMCIDIN AND THE INTERACTION OF NF-KB (P50 AND P65) WITH THEIR SMALL INHIBITORS
Authors: NGUYEN VAN SANG
Keywords: Dermcidin, NF-kappaB, P50, P65, Andrographolide, Parthenolide
Issue Date: 24-Jan-2013
Source: NGUYEN VAN SANG (2013-01-24). STRUCTURAL STUDIES OF THE HUMAN ANTIMICROBIAL PEPTIDE DERMCIDIN AND THE INTERACTION OF NF-KB (P50 AND P65) WITH THEIR SMALL INHIBITORS. ScholarBank@NUS Repository.
Abstract: Project 1: Human antimicrobial peptide dermcidin (DCD) kills a broad spectrum of microorganism. In sweat, DCD peptide is proteolytically processed into fourteen DCD peptides. In this study, three DCD isoform 1 peptides (DCD-1L, SSL-29, SSL-25) and DCD isoform 2 (DCD-2) peptide are chosen for functional and structural studies as they have distinct isoelectric points (pI) and net charges. We determined the 3D structures of DCD-1L, SSL-29, SSL-25 and DCD-2 in SDS using NMR spectroscopy and elucidated the membrane/DCD peptides interaction using biophysical methods. Project 2: NF-kappaB is a transcription factor that controls over 500 genes and plays a key role in regulating human immune system. Dysregulation of NF-kappaB is associated with many human diseases including atopic dermatitis and asthma. In this study, we elucidated the interaction of the two most dominant NF-kappaB (P50 and P65) with their inhibitors, andrographolide and parthenolide.
URI: http://scholarbank.nus.edu.sg/handle/10635/42969
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