Structure–activity relationships in β‐defensin peptides

Abstract

The β‐defensins comprise a large family of small cationic antimicrobial peptides widely distributed in plants, mammals and insects. These cysteine rich peptides display multifunctional properties with implications as potential therapeutic agents. Recent research has highlighted their role in both the innate and adaptive immune systems as well as being novel melanocortin ligands. Studies investigating structure and function provide an insight into the molecular basis of their immunological properties. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 90: 1–7, 2008. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

A new bioproduction route for a novel antimicrobial peptide

“…6b). The killing mechanism of hBD28 revealed from these results agree well with the ''carpet model,'' which has been proposed to describe the antimicrobial activity of b-defensins (Pazgiera et al, 2006;Taylor et al, 2007). In the ''carpet model,'' the accumulation and eventual aggregation of peptides at the bacterial membrane are required for effective pore formation (Brogden, 2005).…”

The first chordate big defensin: Identification, expression and bioactivity

“…Antimicrobial peptides (AMPs) are ancient innate immune components and have been identified in organisms throughout the plant and animal kingdoms. Defensins constitute a family of AMPs with antimicrobial activity and immunomodulatory property [1,2]. Based on their disulfide patterns, defensins are classified into three subfamilies, a-, b-and q-defensins.…”

“…Most defensins are small peptides (12e50 amino acids), display cationic property and possess an amphipathic (containing both hydrophobic and hydrophilic domains) structure, enabling them to interact with microbial membranes [2,11]. Interestingly, a defensin consisting of 79 amino acids, termed big defensin, was also purified from the horseshoe crab Tachypleus tridentatus by Saito et al [12].…”

Human Beta Defensins 1, 2 and 3 Produced by Amniochorion Membranes Is Similar in Term and Preterm Delivery

“…Additionally, HBDs are mainly effective against gram-negative and grampositive bacteria and yeast, but this microbial activity against bacteria is not the same for these defensins, in which HBD1 and 2 are predominantly against gramnegative bacteria and yeasts [21] [23], HBD4 is effective against gram-negative and gram-positive bacteria [24] and HBD3 is active for all the cited microorganisms [21]. The antimicrobial activity is explained by the ability to the HBD2, for example, to inhibit the LPS action and block the inflammation by the LPS-induced TNF-α production [25].…”