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- Title
Lactoferrampin, an antimicrobial peptide of bovine lactoferrin, exerts its candidacidal activity by a cluster of positively charged residues at the C-terminus in combination with a helix-facilitating N-terminal part.
- Authors
Van der Kraan, Marieke I. A.; Nazmi, Kamran; Teeken, Afke; Groenink, Jasper; Van 't Hof, Wim; Veerman, Enno C.I.; Bolscher, Jan G.M.; Nieuw Amerongen, Arie V.
- Abstract
The antimicrobial activity of bovine lactoferrin (bLF) is attributed to lactoferricin, which is situated in the N1-domain of bLF. Recently, another antimicrobial domain consisting of residues 268-284, designated lactoferrampin (LFampin), has been identified in the N1-domain of bLF, which exhibited antimicrobial activity against Candida albicans and several bacteria. In the present study, the candidacidal activity of a series of peptides spanning this antimicrobial domain was investigated in relation to the charge and the capacity to form a helical conformation in hydrophobic environments. C-Terminal truncation of LFampin resulted in a drastic decrease in candidacidal activity. Positively charged residues clustered at the C-terminal side of the LFampin domain appeared to be crucial for the candidacidal activity. The ability to adopt helical conformations did not change when LFampin was truncated at the C-terminal side. N-Terminally truncated LFampin peptides, truncated up to the sequence 270-284, were more reluctant to adopt a helical conformation. Therefore, we conclude that the C-terminal part of LFampin 265-284, which is the most active peptide, is crucial for its candidacidal activity, due to the presence of clustered positive charges, and that the N-terminal part is essential for activity as it facilitates helix formation.
- Subjects
PEPTIDES; LACTOFERRIN; IRON proteins; CANDIDA albicans; BIOCHEMISTRY
- Publication
Biological Chemistry, 2005, Vol 386, Issue 2, p137
- ISSN
1431-6730
- Publication type
Article
- DOI
10.1515/BC.2005.017