The interaction and orientation of Peptide KL4 in model membranes.
Biochim Biophys Acta Biomembr
; 1864(7): 183893, 2022 07 01.
Article
em En
| MEDLINE
| ID: mdl-35219719
ABSTRACT
We report on the orientation and location of synthetic pulmonary surfactant peptide KL4, (KLLLL)4K, in model lipid membranes. The partitioning depths of selectively deuterated leucine residues within KL4 were determined in DPPCPOPG (41) and POPCPOPG (41) bilayers by oriented neutron diffraction. These measurements were combined with an NMR-generated model of the peptide structure to determine the orientation and partitioning of the peptide at the lipid-water interface. The results demonstrate KL4 adopting an orientation that interacts with a single membrane leaflet. These observations are consistent with past 2H NMR and EPR studies (Antharam et al., 2009; Turner et al., 2014).
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosfatidilgliceróis
/
Peptídeos e Proteínas de Sinalização Intercelular
Tipo de estudo:
Prognostic_studies
Idioma:
En
Ano de publicação:
2022
Tipo de documento:
Article