Marieke I.A. van der Kraan, 1. Department of Oral Biochemistry, Academic Center for Dentistry Amsterdam (ACTA), ‘Vrije Universiteit’ and ‘Universiteit van Amsterdam’, Van der Boechorststraat 7, NL-1081 BT Amsterdam, The Netherlands
1 Kamran Nazmi, 2. Department of Oral Biochemistry, Academic Center for Dentistry Amsterdam (ACTA), ‘Vrije Universiteit’ and ‘Universiteit van Amsterdam’, Van der Boechorststraat 7, NL-1081 BT Amsterdam, The Netherlands
2 Afke Teeken, 3. Department of Oral Biochemistry, Academic Center for Dentistry Amsterdam (ACTA), ‘Vrije Universiteit’ and ‘Universiteit van Amsterdam’, Van der Boechorststraat 7, NL-1081 BT Amsterdam, The Netherlands
3 Jasper Groenink, 4. Department of Oral Biochemistry, Academic Center for Dentistry Amsterdam (ACTA), ‘Vrije Universiteit’ and ‘Universiteit van Amsterdam’, Van der Boechorststraat 7, NL-1081 BT Amsterdam, The Netherlands
4 Wim van 't Hof, 5. Department of Oral Biochemistry, Academic Center for Dentistry Amsterdam (ACTA), ‘Vrije Universiteit’ and ‘Universiteit van Amsterdam’, Van der Boechorststraat 7, NL-1081 BT Amsterdam, The Netherlands
5 Enno C.I. Veerman, 6. Department of Oral Biochemistry, Academic Center for Dentistry Amsterdam (ACTA), ‘Vrije Universiteit’ and ‘Universiteit van Amsterdam’, Van der Boechorststraat 7, NL-1081 BT Amsterdam, The Netherlands
6 Jan G.M. Bolscher, 7. Department of Oral Biochemistry, Academic Center for Dentistry Amsterdam (ACTA), ‘Vrije Universiteit’ and ‘Universiteit van Amsterdam’, Van der Boechorststraat 7, NL-1081 BT Amsterdam, The Netherlands
7 Arie V. Nieuw Amerongen8. Department of Oral Biochemistry, Academic Center for Dentistry Amsterdam (ACTA), ‘Vrije Universiteit’ and ‘Universiteit van Amsterdam’, Van der Boechorststraat 7, NL-1081 BT Amsterdam, The Netherlands
8 Corresponding author
Citation Information. Biological Chemistry. Volume 386, Issue 2, Pages 137–142, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2005.017, February 2005
Publication History: Received: //; accepted: //; published online: 01/06/2005
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.
Keywords α-helix, amphipathicity, antimicrobial peptide, Candida albicans, lactoferrampin, lactoferrin
