Single Lipid Bilayers Constructed on Polymer Cushion Studied by Sum Frequency Generation Vibrational Spectroscopy

Wang, Ting; Li, Dawei; Lü, Xiaolin; Khmaladze, Alexander; Han, Xiaofeng; Ye, Shuji; Yang, Pei; Xue, Gi; He, Nongyue; Chen, Zhan

doi:10.1021/jp200546h

Cited by 39 publications

(52 citation statements)

References 72 publications

(121 reference statements)

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“…Solid supported lipid bilayers have been used in previous SFG studies [45][46][47][48][49][50][51][52][53]. Here, isotope labels can also be used to spectroscopically separate different regions within the model membrane.…”

Section: Resultsmentioning

confidence: 99%

SAP(E) – A cell-penetrating polyproline helix at lipid interfaces

Franz

Lelle

Peneva

et al. 2016

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Cell-penetrating peptides (CPPs) are short membrane-permeating amino acid sequences that can be used to deliver cargoes, e.g. drugs, into cells. The mechanism for CPP internalization is still subject of ongoing research. An interesting family of CPPs is the sweet arrow peptides - SAP(E) - which are known to adopt a polyproline II helical secondary structure. SAP(E) peptides stand out among CPPs because they carry a net negative charge while most CPPs are positively charged, the latter being conducive to electrostatic interaction with generally negatively charged membranes. For SAP(E)s, an internalization mechanism has been proposed, based on polypeptide aggregation on the cell surface, followed by an endocytic uptake. However, this process has not yet been observed directly - since peptide-membrane interactions are inherently difficult to monitor on a molecular scale. Here, we use sum frequency generation (SFG) vibrational spectroscopy to investigate molecular interactions of SAP(E) with differently charged model membranes, in both mono- and bi-layer configurations. The data suggest that the initial binding mechanism is accompanied by structural changes of the peptide. Also, the peptide-model membrane interaction depends on the charge of the lipid headgroup with phosphocholine being a favorable binding site. Moreover, while direct penetration has also been observed for some CPPs, the spectroscopy reveals that for SAP(E), its interaction with model membranes remains limited to the headgroup region, and insertion into the hydrophobic core of the lipid layer does not occur.

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Section: Resultsmentioning

confidence: 99%

SAP(E) – A cell-penetrating polyproline helix at lipid interfaces

Franz

Lelle

Peneva

et al. 2016

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…The Chen group has examined membrane perturbations of solid supported bilayers induced by antimicrobial peptides [172–175], membrane-active polymers [174], melittin [176], and magainin [177]. Recently, Chen and co-workers have expanded to cushioned supported bilayers, specifically investigating poly( l -lactic acid) (PLLA) supported PG bilayers and their interaction with Cecropin P1, an antimicrobial peptide [178]. Chen and co-workers have further probed the orientation of the G protein β subunit [179], melittin [180], antimicrobial peptides [175,179–182], alamethicin [183], tachyplesin I [184], and cytochrome b5 [185], embedded within various bilayers.…”

Section: Methods To Study the Interactions Of Nonclassically Releamentioning

confidence: 99%

Protein-Phospholipid Interactions in Nonclassical Protein Secretion: Problem and Methods of Study

Prudovsky

Kumar

Sterling

et al. 2013

IJMS

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Extracellular proteins devoid of signal peptides use nonclassical secretion mechanisms for their export. These mechanisms are independent of the endoplasmic reticulum and Golgi. Some nonclassically released proteins, particularly fibroblast growth factors (FGF) 1 and 2, are exported as a result of their direct translocation through the cell membrane. This process requires specific interactions of released proteins with membrane phospholipids. In this review written by a cell biologist, a structural biologist and two membrane engineers, we discuss the following subjects: (i) Phenomenon of nonclassical protein release and its biological significance; (ii) Composition of the FGF1 multiprotein release complex (MRC); (iii) The relationship between FGF1 export and acidic phospholipid externalization; (iv) Interactions of FGF1 MRC components with acidic phospholipids; (v) Methods to study the transmembrane translocation of proteins; (vi) Membrane models to study nonclassical protein release.

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“…In another example of cell membrane model with adsorbed films on solid substrates, Wang et al [135] replaced an inorganic-lipid interface by an organic-lipid one. They examined and compared single lipid bilayers of DPPG and dDPPG assembled on solid surfaces of CaF 2 (inorganiclipid interface) and on a poly(lactic acid) (PLLA) cushion (organic-lipid interface).…”

Section: Films Deposited On Solid Substratesmentioning

confidence: 99%

“…The inset shows the IR and visible beams crossing unwanted interfaces and reaching the desired one, where the SFG beam is generated. Reprinted adapted with permission from [135]. Copyright 2014 American Chemical Society.…”

Section: Probing Surface Functionalizationmentioning

confidence: 99%