Abstract:
:Antimicrobial peptides (AMPs) and mucins are components of airway secretions and both contribute to the innate host defense system. At neutral pH, AMPs are positively charged, mucins negatively. It was the aim of the study to test whether these opposite charges result in interactions between AMPs and mucins. We measured binding of mucins isolated from porcine gastric mucosa to the cathelicidin LL-37 coated to multiwell plates and found that LL-37 electrostatically interacts with mucins. Circular dichroism spectra of the peptide revealed the induction of alpha-helical conformation by mucins. Addition of mucins to solutions of LL-37 significantly decreased the antimicrobial activity of the peptide against Pseudomonas aeruginosa and Streptococcus pneumoniae. We then tested whether LL-37 is bound to mucins in airway secretions from human subjects and found that a significant proportion of the peptide and its propeptide are bound to high molecular weight components. Together these data show that cationic AMPs interact with anionic mucins in airway secretions. Functions of AMPs are modulated by this interaction.
journal_name
Peptidesjournal_title
Peptidesauthors
Felgentreff K,Beisswenger C,Griese M,Gulder T,Bringmann G,Bals Rdoi
10.1016/j.peptides.2006.07.018subject
Has Abstractpub_date
2006-12-01 00:00:00pages
3100-6issue
12eissn
0196-9781issn
1873-5169pii
S0196-9781(06)00345-7journal_volume
27pub_type
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