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Structure–activity relationship of human liver-expressed antimicrobial peptide 2

✍ Scribed by Agnès Hocquellet; Benoit Odaert; Charlotte Cabanne; Abdelmajid Noubhani; Wilfrid Dieryck; Gilles Joucla; Caroline Le Senechal; Milen Milenkov; Stéphane Chaignepain; Jean-Marie Schmitter; Stéphane Claverol; Xavier Santarelli; Erick J. Dufourc; Marc Bonneu; Bertrand Garbay; Patricia Costaglioli

Book ID
116832064
Publisher
Elsevier Science
Year
2010
Tongue
English
Weight
621 KB
Volume
31
Category
Article
ISSN
0196-9781

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Structure-activity relationship of HP (2
Structure-activity relationship of HP (2–20) analog peptide: Enhanced antimicrobial activity by N-terminal random coil region deletion
✍ Yoonkyung Park; Seong-Cheol Park; Hae-Kyun Park; Song Yub Shin; Yangmee Kim; Kyu 📂 Article 📅 2007 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 438 KB

## Abstract HP (2–20) (AKKVFKRLEKLFSKIQNDK) is a 19‐aa antimicrobial peptide derived from N‐terminus of __Helicobacter pylori__ Ribosomal protein L1 (RpL1). In the previous study, several analogs with amino acid substitutions were designed to increase or decrease only the net hydrophobicity. In par