Studies on the assembly of a leucine zipper antibacterial peptide and its analogs onto mammalian cells and bacteria
Author:
Publisher
Springer Science and Business Media LLC
Subject
Organic Chemistry,Clinical Biochemistry,Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/s00726-010-0744-7.pdf
Reference41 articles.
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2. Ahmad A, Asthana N, Azmi S, Srivastava RM, Pandey BK, Yadav V, Ghosh JK (2009a) Structure-function study of cathelicidin-derived bovine antimicrobial peptide BMAP-28: design of its cell-selective analogs by amino acid substitutions in the heptad repeat sequences. Biochim Biophys Acta 1788:2411–2420
3. Ahmad A, Azmi S, Srivastava RM, Srivastava S, Pandey BK, Saxena R, Bajpai VK, Ghosh JK (2009b) Design of nontoxic analogues of cathelicidin-derived bovine antimicrobial peptide BMAP-27: the role of leucine as well as phenylalanine zipper sequences in determining its toxicity. Biochemistry 48:10905–10917
4. Asthana N, Yadav SP, Ghosh JK (2004) Dissection of antibacterial and toxic activity of melittin: a leucine zipper motif plays a crucial role in determining its hemolytic activity but not antibacterial activity. J Biol Chem 279:55042–55050
5. Bilgicer B, Kumar K (2004) De novo design of defined helical bundles in membrane environments. Proc Natl Acad Sci USA 101:15324–15329
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