HI Andre, where did you get your information from? I am very interested in the statement you made... Many thanks

Dear Elena, I found this information in the paper below:

Banaschewski, B. J., Veldhuizen, E. J., Keating, E., Haagsman, H. P.,

Zuo, Y. Y., Yamashita, C. M., Veldhuizen, R. A. Antimicrob. Agents

Chemother. 2015, 59, 3075–3083.

I posted this question sometime ago. Now, I have a clue about the real answer. And, I recently submitted it to publication in the Colloid and Surfaces B: Interfaces journal. This manuscript is now under review in the journal. We tried to avoid the direct interaction of antimicrobial peptides with the lung surfactant using a peptide nanocarrier in order to help it penetrating the lung surfactant monolayer barrier. When it is published, I will post it here. In the future, we will test using in vitro experiments.

Please, let me know about your interest in this statement.

Best regards,

Andre Pimentel

Hi, I'm sorry, I just saw this question now.

Our experiments found that certain phospholipids within the surfactant bind to antimicrobial peptides, thereby preventing AMP interaction with bacterial membranes for cytotoxic activities.

If you have any questions, or want to speak more about it, please feel free to contact me directly by e-mail.

- Brandon

We intend to vary the dppg contend in the film in the next project with defensins. I have discussed our ideas with Ruud. I hope we can meet each other in the near future and do some collaboration in this matter.

Most of the antimicrobial peptides are cationic in nature, while there is a list of anionic surfactant, containing anionic functional group at their head (sulfate, sulfonate, phosphate, and carboxylates etc). The binding of surfactant to the AMP prevents them to interact with the cell membrane.