Directionally Aligned Helical Peptides on Surfaces

Whitesell, James K.; Chang, Hye Kyung

doi:10.1126/science.261.5117.73

Cited by 198 publications

(163 citation statements)

References 16 publications

(2 reference statements)

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“…The "grafting-from" approach makes possible the directional alignment of the helical molecules (Fig. 1), as was first demonstrated by the work of Whitesell and Chang (6). These investigators first decorated the surface of a flat metal or metal oxide film with a layer of organic material exhibiting free amino groups by a self-assembly process and then started the polymerization of N-carboxyanhydrides of ␣-Lamino acids (NCAs) to obtain poly-L-amino acids.…”

mentioning

confidence: 82%

Electromechanical Properties of an Ultrathin Layer of Directionally Aligned Helical Polypeptides

Jaworek

Neher

Wegner

et al. 1998

Science

138

104

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mentioning

confidence: 82%

Electromechanical Properties of an Ultrathin Layer of Directionally Aligned Helical Polypeptides

Jaworek

Neher

Wegner

et al. 1998

Science

138

104

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“…Some of the bands corresponding to the apatite (P-O at 1050 cm −1 , and for carbonate group 1420 and 1470 cm −1 ) and the collagen "amide I" and "amide II" ("A I" and "A II" respectively) are shown. [37]. Indeed the amide region is dependent on cross-links to the mineral [38].…”

Section: Ftir Spectramentioning

confidence: 99%

Thermal, infrared spectroscopy and molecular modeling characterization of bone: An insight in the apatite-collagen type I interaction

Heredia¹,

Colín-García²,

Peña‐Rico³

et al. 2013

ABC

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An insight into the interaction of collagen type I with apatite in bone tissue was performed by using differential scanning calorimetry, Fourier transform infrared spectroscopy, and molecular modeling. Scanning electron microscopy shows that bone organic content incinerate gradually through the different temperatures studied. We suggest that the amide regions of the type I collagen molecule (mainly C=O groups of the peptide bonds) will be important in the control of the interactions with the apatite from bone. The amide I infrared bands of the collagen type I change when interacting to apatite, what might confirm our assumption. Bone tissue results in a loss of thermal stability compared to the collagen studied apart, as a consequence of the degradation and further combustion of the collagen in contact with the apatite microcrystals in bone. The thermal behavior of bone is very distinctive. Its main typical combustion temperature is at 360˚C with a shoulder at 550˚C compared to the thermal behavior of collagen, with the mean combustion peak at ca. 500˚C. Our studies with molecular mechanics (MM+ force field) showed different interaction energies of the collagen-like molecule and different models of the apatite crystal planes. We used models of the apatite (100) and (001) planes; additional two planes (001) were explored with phosphate-rich and calcium-rich faces; an energetic preference was found in the latter case. We preliminary conclude that the peptide bond of collagen type I is modified when the molecule interacts with the apatite, producing a decrease in the main peak from ca. 500˚C in collagen, up to 350˚C in bone. The combustion might be related to collagen type I, as the ΔH energies present only small variations between mineralized and non-mineralized samples. The data obtained here give a molecular perspective into the structural properties of bone and the change in collagen properties caused by the interaction with the apatite. Our study can be useful to understand the biological synthesis of minerals as well as the organic-inorganic interaction and the synthesis of apatite implant materials.

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“…This is accomplished by first modifying the surface with initiators for subsequent the polymer synthesis, and then growing a helical chain that is tethered to the surface (grafting from approach) [39], [40]. Surface polymerization to produce PBLG monomolecular films has been performed in the melt [41], in solution [40], [42]- [45], and by a vapor deposition polymerization [46].…”

Section: Pblg Monomolecular Filmsmentioning

confidence: 99%

Sum-frequency spectroscopy and imaging of aligned helical polypeptides

Knoesen

Pakalnis

Zhao

et al. 2004

IEEE J. Select. Topics Quantum Electron.

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Abstract-The sum-frequency spectroscopy signatures of NH-(amide A) and C = O (amide I) groups, the amide segments in all proteins, are measured in thin films that consist of an ensemble of right-handed, helical poly--benzyl-L-glutamate (PBLG) macromolecules that are endgrafted and self-organized into a monomolecular film with a large degree of unidirectional order. Distinct sum-frequency spectral signatures associated with the amide A and the amide I bands are observed because of a strong noncentro-symmetry produced by intra-and intermolecular forces. Hydrogen bonding self-organizes amino and acidic groups within the molecular helical scaffold. In an endgrafted thin film, repulsive electrostatic forces between PBLG macromolecules stabilize the organization between molecules. The average orientation of the PBLG chain was measured. Imaging scans using sum-frequency generation, complemented by atomic force microscopy, were used to investigate the uniformity of orientation of the PBLG chains.

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Directionally Aligned Helical Peptides on Surfaces

Cited by 198 publications

References 16 publications

Electromechanical Properties of an Ultrathin Layer of Directionally Aligned Helical Polypeptides

Electromechanical Properties of an Ultrathin Layer of Directionally Aligned Helical Polypeptides

Thermal, infrared spectroscopy and molecular modeling characterization of bone: An insight in the apatite-collagen type I interaction

Sum-frequency spectroscopy and imaging of aligned helical polypeptides

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