Antibacterial activities and conformations of synthetic alpha-defensin HNP-1 and analogs with one, two and three disulfide bridges.

@article{Mandal2002AntibacterialAA,
  title={Antibacterial activities and conformations of synthetic alpha-defensin HNP-1 and analogs with one, two and three disulfide bridges.},
  author={Manabendra Mandal and Ramakrishnan Nagaraj},
  journal={The journal of peptide research : official journal of the American Peptide Society},
  year={2002},
  volume={59 3},
  pages={95-104}
}
Structure and biological activities of synthetic peptides corresponding to human alpha-defensin HNP-1, AC1YC2RIPAC3IAGERRYGTC4IYQGRLWAFC5C6 with the S-S connectivities: C1-C6, C2-C4, C3-C5, and its variants with one, two and three disulfide bridges were investigated. Oxidation of synthetic, reduced HNP-1 yielded a peptide with S-S connectivities C1-C3, C2-C4 and C5-C6, and not with the S-S linkages as in naturally occurring HNP-1. Selective protection of cysteine sulfhydryls was necessary for… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 33 extracted citations

Optimization of the Oxidative Folding Reaction and Disulfide Structure Determination of Human α-Defensin 1, 2, 3 and 5

International Journal of Peptide Research and Therapeutics • 2008
View 4 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…