Distinct bactericidal activities of bovine lactoferrin peptides LFampin 268-284 and LFampin 265-284: Asp-Leu-Ile makes a difference. |
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| Authors: | Marieke I A van der Kraan Kamran Nazmi Wim van 't Hof Arie V Nieuw Amerongen Enno C I Veerman Jan G M Bolscher |
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| Institution: | Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam (ACTA), Van der Boechorststraat 7, 1081 BT Amsterdam, Netherlands. |
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| Abstract: | 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 of 265Asp-Leu-267Ile did not simply lead to an overall increased potency, since higher concentrations of LFampin 265-284 than LFampin 268-284 were needed to kill the Gram-negative bacteria that were tested. The Asp-Leu-Ile sequence enhances the propensity of LFampin to adopt an alpha-helix, as shown by circular dichroism spectroscopy. These results suggest that the helical conformation of the peptide is an important determinant of the susceptibility of Gram-positive bacteria. |
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