Enno Klüver

TL;DR: Findings demonstrate the existence of a family of β‐defensin genes with different functions against diverse classes of microorganisms, regulated by different stimuli, and specific signal pathways, and confirm the relevance of antimicrobial peptides in host defense.

TL;DR: It is shown that screening of genomic sequences is a valuable tool with which to identify novel regulatory peptides in β-defensins, a family of antimicrobial peptides differentially expressed in most tissues, regulated by specific mechanisms, and exerting physiological functions not only related to direct host defense.

TL;DR: It is found that it is not important for antimicrobial and cytotoxic activity whether and how cysteine residues are arranged to form disulfide bonds, and the antimicrobial potency of hBD-3 peptides is determined by the distribution of positively charged amino acid residues and hydrophobic side chains.

TL;DR: It is significant that β‐defensins do not exhibit a common pattern of charged and hydrophobic residues on the protein surface and that the β‐ defensin‐specific fold appears to accommodate a wide range of different amino acids at most sequence positions.

TL;DR: From human blood ultrafiltrate, a novel gene‐encoded, cysteine‐rich, and cationic peptide is characterized that is termed liver‐expressed antimicrobial peptide 2 (LEAP‐2), a unique peptide that does not exhibit similarity with any known human peptide regarding its primary structure, disulfide motif, and expression.