Partitioning, dynamics, and orientation of lung surfactant peptide KL(4) in phospholipid bilayers.
Partitioning, dynamics, and orientation of lung surfactant peptide KL(4) in phospholipid bilayers.
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磷脂双层中肺表面活性剂肽KL（4）的分配，动力学和方向。
DOI：
10.1016/j.bbamem.2009.08.020
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发表时间：
2010-02
影响因子：
3.4
通讯作者：
Farver, R. Suzanne
中科院分区：
文献类型：
--
作者：
Long, Joanna R.;Mills, Frank D.;Ganesh, Omjoy K.;Antharam, Vijay C.;Farver, R. Suzanne
关键词：
Lung surfactant protein B (SP-B) is a lipophilic protein critical to lung function at ambient pressure. KL4 is a 21-residue peptide which has successfully replaced SP-B in clinical trials of synthetic lung surfactants. CD and FTIR measurements indicate KL4 is helical in a lipid bilayer environment, but its exact secondary structure and orientation within the bilayer remain controversial. To investigate the partitioning and dynamics of KL4 in phospholipid bilayers, we introduced CD3-enriched leucines at four positions along the peptide to serve as probes of sidechain dynamics via 2H solid-state NMR. The chosen labels allow distinction between models of helical secondary structure as well as between a transmembrane orientation or partitioning in the plane of the lipid leaflets. Leucine sidechains are also sensitive to helix packing interactions in peptides that oligomerize. The partitioning and orientation of KL4 in DPPC/POPG and POPC/POPG phospholipid bilayers, as inferred from the leucine sidechain dynamics, is consistent with monomeric KL4 lying in the plane of the bilayers and adopting an unusual helical structure which confers amphipathicity and allows partitioning into the lipid hydrophobic interior. At physiologic temperatures, the partitioning depth and dynamics of the peptide are dependent on the degree of saturation present in the lipids. The deeper partitioning of KL4 relative to antimicrobial amphipathic α-helices leads to negative membrane curvature strain as evidenced by the formation of hexagonal phase structures in a POPE/POPG phospholipid mixture on addition of KL4. The unusual secondary structure of KL4 and its ability to differentially partition into lipid lamellae containing varying levels of saturation suggest a mechanism for its role in restoring lung compliance.
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影响因子：
3.4
作者：
Antharam, Vijay C.;Elliott, Douglas W.;Long, Joanna R.
通讯作者：
Long, Joanna R.
影响因子：
2.9
作者：
Booth, V;Waring, AJ;Keough, KMW
通讯作者：
Keough, KMW
DOI：
10.1073/pnas.88.16.7451
发表时间：
1991-08-01
影响因子：
11.1
作者：
BRUNI, R;TAEUSCH, HW;WARING, AJ
通讯作者：
WARING, AJ
DOI：
10.1164/ajrccm.153.1.8542150
发表时间：
1996-01-01
影响因子：
24.7
作者：
Cochrane, CG;Revak, SD;Alberts, MS
通讯作者：
Alberts, MS
影响因子：
3.4
作者：
Martinez-Gil, Luis;Perez-Gil, Jesus;Mingarro, Ismael
通讯作者：
Mingarro, Ismael