Self-Assembling Porphyrin-Modified Peptides

Dunetz, Joshua R.; Sandstrom, Claire; Young, Elizabeth R.; Baker, Paul K.; Name, Steven A. Van; Cathopolous, Terry; Fairman, Robert; Paula, Julio C. de; Åkerfeldt, Karin S.

doi:10.1021/ol050644h

Cited by 46 publications

(39 citation statements)

References 23 publications

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“…In nature, elegant arrangements of peptide–porphyrin conjugates are essential in conducting biological processes . This has inspired researchers worldwide to investigate the self‐assembly and supramolecular structures of porphyrin–peptide conjugates mimicking the structure and role of natural porphyrin . In this work, we explore the development and use of l ‐ and d ‐phenylalanine‐substituted protoporphyrin IX derivatives 1 and 2 , respectively, for the solvophobic‐controlled assembly of nanostructures (Figure ).…”

Section: Introductionmentioning

confidence: 99%

Solvent‐Tuned Self‐Assembled Nanostructures of Chiral l/d‐Phenylalanine Derivatives of Protoporphyrin IX

et al. 2015

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Protoporphyrin IX is a naturally occurring amphiphilic porphyrin with a rigid hydrophobic nonpolar core and two polar propionic acid substitutions on the porphyrin ring. This molecule can be modified on the hydrophilic group, which can lead to strengthened π–π-stacking and spontaneous self-assembly into novel nanostructures. Herein, we use l- phenylalanine and d-phenylalanine to modify protoporphyrin IX, and use the two derivatives for solvophobic-controlled self-assembly. Both derivatives possess two important features: 1) the aromatic core of the porphyrin for dispersive interactions and 2) a chiral amino acid to maximize the influence of chirality on selfassembly. These derivatives lead to the formation of a variety of nanostructure morphologies, such as spheres, nanofibers, lamellar structures, and thread-like and spherical shells. Solution-based self-assembly was determined by UV/Vis, fluorescence, and circular dichroism spectroscopy, and the formed nanostructures were characterized by scanning electron microscopy (SEM). Such engineered porphyrin derivatives could have potential applications in energy transport and storage, supramolecular chemistry, materials science, and medicine.

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Section: Introductionmentioning

confidence: 99%

Solvent‐Tuned Self‐Assembled Nanostructures of Chiral l/d‐Phenylalanine Derivatives of Protoporphyrin IX

et al. 2015

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“…In other words, protein scaffolds hold pigments at intermolecular distances that optimize electronic coupling, photon capture and energy transfer. [1][2][3] Therefore, a precise arrangement of photofunctional molecules on a molecular scale is essential for artificial photoenergy conversion systems.…”

Section: Introductionmentioning

confidence: 99%

First Cellulose Langmuir‐Blodgett Films towards Photocurrent Generation Systems

Sakakibara

Ogawa

Nakatsubo

2007

Macromol. Rapid Commun.

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Langmuir‐Blodgett films of a cellulose derivative containing porphyrins, porphyrin‐cellulose, were fabricated in order to construct a cellulose‐based molecular photocurrent generation system. On visible light illumination of the LB monolayer film deposited on an ITO electrode, anodic photocurrents were observed with a quantum yield of 1.6% at an applied potential of 0 V versus SCE, and 3.8–4.6% at 0.2–0.3 V versus SCE. These values indicate that the self‐quenching of the photoexcited porphyrins in the cellulose LB film was suppressed, while porphyrin moieties in the LB film had a densely packed structure. This is because the porphyrins are located at a distance of approximately 1.0 nm along the cellulose backbone.magnified image

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“…S2). Red shifting is an artifact of increased light scattering, which decreases the extinction nonlinearly with decreasing wavelength 37–40. Interestingly, simply inverting the cuvette several times results in dissolution of the large aggregates while retaining all of the β‐sheet characteristics, suggesting that the material is readily reversible.…”

Section: Resultsmentioning

confidence: 99%

Polyglutamine fibrils are formed using a simple designed β‐hairpin model

et al. 2010

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Polyglutamine repeats are found in proteins associated with many neurodegenerative diseases. These repeats are responsible for intracellular protein aggregation that resemble amyloid plaques and contain the hallmarks of cross-beta fibrillar structures. Recent work has suggested that the glutamines are involved in aggregation through two possible mechanisms: one involving only side-chain hydrogen bonding and a second involving interdigitation of the glutamines with tight van der Waal's packing (steric zipper model). We are interested in determining which interactions are particularly involved in early assembly processes and have developed a beta-hairpin model system to address this problem. Our model system is designed to stabilize a putative high-energy nucleating structure to provide a window to view early assembly processes. We have applied spectroscopy tools (circular dichroism, infrared, and dynamic light scattering) to probe the self-assembly of beta-sheet fibrils. These experiments established the conditions to study fibrillar morphology using atomic force microscopy. We show that fibrils are short with minimal lateral growth, suggesting that this may be a good model system for studying early assembly steps.

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Self-Assembling Porphyrin-Modified Peptides

Cited by 46 publications

References 23 publications

Solvent‐Tuned Self‐Assembled Nanostructures of Chiral l/d‐Phenylalanine Derivatives of Protoporphyrin IX

Solvent‐Tuned Self‐Assembled Nanostructures of Chiral l/d‐Phenylalanine Derivatives of Protoporphyrin IX

First Cellulose Langmuir‐Blodgett Films towards Photocurrent Generation Systems

Polyglutamine fibrils are formed using a simple designed β‐hairpin model

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