Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Marieke I.A. van der Kraan"'
Autor:
Enno C. I. Veerman, Jan G. M. Bolscher, Wim van 't Hof, Arie V. Nieuw Amerongen, Kamran Nazmi, Marieke I.A. van der Kraan
Publikováno v:
Biochemistry and Cell Biology. 84:358-362
Two lactoferrampin (LFampin) peptides derived from bovine lactoferrin were compared with respect to their bactericidal activities. LFampin 265–284 killed a set of Gram-positive bacteria that were resistant to LFampin 268–284. The presence of265As
Autor:
Marieke I.A. van der Kraan, Kamran Nazmi, Arie V. Nieuw Amerongen, Enno C. I. Veerman, Christel van der Made, Jan G. M. Bolscher, J. Groenink, Wim van 't Hof
Publikováno v:
Peptides. 26:2093-2097
LFampin 265-284, derived from bovine lactoferrin, has broad-spectrum antimicrobial activity against the yeast Candida albicans and several Gram-positive and Gram-negative bacteria. A glycine substitution scan was used to identify residues that are im
Autor:
Wim van 't Hof, Enno C. I. Veerman, Arie V. Nieuw Amerongen, Kamran Nazmi, Marieke I.A. van der Kraan, Jan G. M. Bolscher, Jan van Marle, J. Groenink
Publikováno v:
Peptides. 26:1537-1542
Antimicrobial peptides allegedly exert their action on microbial membranes. Bovine lactoferrin enfold two antimicrobial domains, lactoferricin B (LFcin B) and lactoferrampin (LFampin). Effects of representative peptides thereof on the membranes of Ca
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
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
Autor:
Kamran Nazmi, Enno C. I. Veerman, Marieke I.A. van der Kraan, Jan G. M. Bolscher, J. Groenink, Arie V. Nieuw Amerongen
Publikováno v:
Peptides, 25, 177-183. Elsevier Inc.
van der Kraan, M I A, Groenink, J, Nazmi, K, Veerman, E C I, Bolscher, J G M & van Nieuw Amerongen, A 2004, ' Lactoferrampin: a novel antimicrobial peptide in the N1-domain of bovine lactoferrin ', Peptides, vol. 25, pp. 177-183 . https://doi.org/10.1016/j.peptides.2003.12.006
Peptides, 25, 177-183. Elsevier
van der Kraan, M I A, Groenink, J, Nazmi, K, Veerman, E C I, Bolscher, J G M & van Nieuw Amerongen, A 2004, ' Lactoferrampin: a novel antimicrobial peptide in the N1-domain of bovine lactoferrin ', Peptides, vol. 25, pp. 177-183 . https://doi.org/10.1016/j.peptides.2003.12.006
Peptides, 25, 177-183. Elsevier
The antimicrobial activity of bovine lactoferrin is attributed to lactoferricin, situated in the N1-domain. Based on common features of antimicrobial peptides, a second putative antimicrobial domain was identified in the N1-domain of lactoferrin, des