PIRSA:13120043

Calculating the free energy of antimicrobial peptide (HHC-36) dimerization in bulk

vafa, S. (2013). Calculating the free energy of antimicrobial peptide (HHC-36) dimerization in bulk. Perimeter Institute. https://pirsa.org/13120043

vafa, shaqa. Calculating the free energy of antimicrobial peptide (HHC-36) dimerization in bulk. Perimeter Institute, Dec. 05, 2013, https://pirsa.org/13120043 

          @misc{ pirsa_PIRSA:13120043,
            doi = {10.48660/13120043},
            url = {https://pirsa.org/13120043},
            author = {vafa, shaqa},
            keywords = {},
            language = {en},
            title = {Calculating the free energy of antimicrobial peptide (HHC-36) dimerization in bulk},
            publisher = {Perimeter Institute},
            year = {2013},
            month = {dec},
            note = {PIRSA:13120043 see, \url{https://pirsa.org}}
          }

shaqa vafa University of Guelph

Talk numberPIRSA:13120043
DOI10.48660/13120043
Collection
Talk Type Conference

Abstract

The increasing demand for antibiotics has contributed to the investigation of possible novel antibiotics by many researchers. For this purpose experimental and theoretical studies have been carried out to draw scientists' attention to antimicrobial peptides and their interaction with the surface of bacterial membranes. Their ability to disrupt the functioning of bacterial membranes has been probed from different perspectives. The most desirable antimicrobial peptides are those which do not harm plant or animals' membranes but which disrupt bacterial membranes. It has been found that some cationic antimicrobial peptides (CAPs) satisfy these requirements. CAPs interacting with the outer membrane of gram-negative bacteria and the membrane of gram-positive bacteria have been studied recently.We conduct a Molecular Dynamics simulation study of peptide-peptide interactions in physiological solutions and investigate the mechanism of CAPs aggregation since aggregation of the peptides could precede their interaction with the membrane. Different algorithms are applied to calculate the potential mean force of the aggregation process of peptides to select the most efficient one. Also we have run CD spectroscopy and calorimetry experiments to predict the structure of the peptide and measure the peptide-peptide binding enthalpy and compared these results with our simulation data. The particular CAP studied is HHC-36 a peptide selected by high throughput screening (A. Cherkasov et al ACS Chem. Biol. 2009 4 (1) pp 6574) (M. Kazemzadeh-Narbat et al Biomed. Mater. Res. Part B 2012 5 pp1344-1352) (M. Ma et al Biomed. Mater. Res. Part A 2012 2 pp278-185) which has nine amino acid residues and charge +5.