The antimicrobial peptide cathelicidin interacts with airway mucus.
Peptides
; 27(12): 3100-6, 2006 Dec.
Article
em En
| MEDLINE
| ID: mdl-16963160
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.
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Base de dados:
MEDLINE
Assunto principal:
Mucosa Respiratória
/
Peptídeos Catiônicos Antimicrobianos
/
Muco
Limite:
Adult
/
Animals
/
Humans
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article