In situ molecular level studies on membrane related peptides and proteins in real time using sum frequency generation vibrational spectroscopy

Interfacial peptides and proteins are critical in many biological processes and thus are of interest to various research fields. To study these processes, surface sensitive techniques are required to completely describe different interfacial interactions intrinsic to many complicated processes. Sum frequency generation (SFG) spectroscopy has been developed into a powerful tool to investigate these interactions and mechanisms of a variety of interfacial peptides and proteins. It has been shown that SFG has intrinsic surface sensitivity and the ability to acquire conformation, orientation and ordering information about these systems. This paper reviews recent studies on peptide/protein-substrate interactions, peptide/protein-membrane interactions and protein complexes at interfaces and demonstrates the ability of SFG on unveiling the molecular pictures of complicated interfacial biological processes.

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“…Through deuteration, we have been able to probe either the bilayer behavior or the response from each leaflet. 82,85 …”

Section: Example Applicationsmentioning

confidence: 99%

Molecular Interactions of Proteins and Peptides at Interfaces Studied by Sum Frequency Generation Vibrational Spectroscopy

2011

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“…By implementing different polarization combinations of the incident and detected beams, different orientational components of the interfacial molecules can be probed. This technique has already been a useful tool for studying charged biological macromolecules at air-water, [39][40][41][42][43][44][45][46] solid-liquid, 39,41,44,45,[47][48][49][50][51][52][53][54] and membrane interfaces; 39,[44][45][46][55][56][57][58][59][60] including, polyelectrolytes at the air-water 61-63 and solid-liquid [64][65][66][67][68][69] interfaces. While informative, these previous VSF studies do not capture the role of a unique oil-water interfacial environment on polyelectrolyte adsorption and assembly.…”

Section: Introductionmentioning

confidence: 99%

Molecular Insights in the Structure and Layered Assembly of Polyelectrolytes at the Oil/Water Interface

Robertson

Richmond

2014

J. Phys. Chem. C

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Macromolecular assembly at the interface between water and a hydrophobic surface underlies some of the most important biological and environmental processes on the planet. Important model systems for understanding this assembly at such interfaces are polyelectrolytes that have hydrophilic units interspersed along a hydrophobic polymer backbone, similar to many biological macromolecules. This feature article provides recent advances in the molecular factors that contribute to the adsorption and assembly of carboxylic acid-containing polyelectrolytes at the carbon tetrachloride-water interface, a model system for an oil-water interface. Using vibrational sum frequency spectroscopy and interfacial tension techniques, these unique set of studies presented herein identify the factors that dictate whether or not polyelectrolytes will adsorb to the oil-water interface, and also describe the specifics of the adsorption process that depend upon factors such as polymer size, charge density, hydrophobicity, conformation and the effect of metal ion electrostatics and bonding.

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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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In situ molecular level studies on membrane related peptides and proteins in real time using sum frequency generation vibrational spectroscopy

Cited by 99 publications

References 205 publications

Molecular Interactions of Proteins and Peptides at Interfaces Studied by Sum Frequency Generation Vibrational Spectroscopy

Molecular Interactions of Proteins and Peptides at Interfaces Studied by Sum Frequency Generation Vibrational Spectroscopy

Molecular Insights in the Structure and Layered Assembly of Polyelectrolytes at the Oil/Water Interface

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

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