Structural and functional characterization of hBD-1(Ser35), a peptide deduced from a DEFB1 polymorphism |
| |
Authors: | Circo Raffaella Skerlavaj Barbara Gennaro Renato Amoroso Antonio Zanetti Margherita |
| |
Affiliation: | Dipartimento di Scienze e Tecnologie Biomediche, Università di Udine, P.le Kolbe, 4, 33100 Udine, Italy. |
| |
Abstract: | beta-Defensins are mammalian antimicrobial peptides that share a unique disulfide-bonding motif of six conserved cysteines. An intragenic polymorphism of the DEFB1 gene that changes a highly conserved Cys to Ser in the peptide coding region has recently been described. The deduced peptide cannot form three disulfide bonds, as one of the cysteines is unpaired. We have determined the cysteine connectivities of a corresponding synthetic hBD-1(Ser35) peptide, investigated the structure by circular dichroism spectroscopy, and assayed the in vitro antimicrobial activity. Despite a different arrangement of the disulfides, hBD-1(Ser35) proved as active as hBD-1 against the microorganisms tested. This activity likely depends on the ability of hBD-1(Ser35) to adopt an amphipathic conformation in hydrophobic environment, similar to the wild type peptide, as suggested by CD spectroscopy. |
| |
Keywords: | Antimicrobial peptide hBD-1 Polymorphic variant Cysteine connectivities Circular dichroism spectroscopy |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|