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

Autor: Arie V. Nieuw Amerongen, Wim van 't Hof, Jan G. M. Bolscher, Enno C. I. Veerman, J. Groenink, Marieke I.A. van der Kraan, Kamran Nazmi, Afke Teeken

Publikováno v: Biological Chemistry, 386, 137-142. Walter de Gruyter GmbH
Biological chemistry, 386, 137-142. De Gruyter
van der Kraan, M I A, Nazmi, K, Teeken, A, Groenink, J, van 't Hof, W, Veerman, E C I, Bolscher, J G M & van Nieuw Amerongen, A 2005, ' 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 ', Biological Chemistry, vol. 386, pp. 137-142 . https://doi.org/10.1515/BC.2005.017

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 i

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https://hdl.handle.net/11245/1.247556