The Effect of Aminoacylated Phospholipids on Membrane Binding of the Antimicrobial Peptides Cecropin a and Mastoparan X
β Scribed by Pagentine, Sarah
- Book ID
- 122268862
- Publisher
- Biophysical Society
- Year
- 2011
- Tongue
- English
- Weight
- 39 KB
- Volume
- 100
- Category
- Article
- ISSN
- 0006-3495
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A 15-residue hybrid peptide ( KWKLFKKIGAVLKVL-amide) incorporating partial sequences of cecropin A and melittin causes the release of carboxyfluoresceine encapsulated in phosphatidylcholine liposomes. Succinylation of the amino groups in the N-terminus and lysine side chains inhibits the effect of t
Short cationic antimicrobial peptides (AMPs) are believed to act either by inducing transmembrane pores or disrupting membranes in a detergent-like manner. For example, the antimicrobial peptides aurein 1.2, citropin 1.1, maculatin 1.1 and caerin 1.1, despite being closely related, appear to act by