Structural investigation of the poly(pentapeptide) of elastin, poly(GVGVP), in the solid state

Rodríguez‐Cabello, José Carlos; Alonso, Matilde; Díez, Mar; Caballero, Moisés Blanco; Herguedas, Mar

doi:10.1002/(sici)1521-3935(19990801)200:8<1831::aid-macp1831>3.0.co;2-v

Cited by 30 publications

(34 citation statements)

References 14 publications

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“…Rodriguez-Cabello et al studied the structure of poly(GVGVP) with thermal, wide-angle XRay diffraction and vibrational Raman analysis. 11 The structure was amorphous with no definite conformation.…”

Section: Methodsmentioning

confidence: 99%

Conformational Characterization of (Val-Pro-Gly-Val-Gly)6 with 13C Solid State NMR

Asakura

Ashida

Ohgo

2003

Polym J

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KEY WORDSElastin / (VPGVG) 6 / 2D Spin-Diffusion Nuclear Magnetic Resonance(NMR) under off Magic Angle Spinning / The repeated pentapeptide sequence, (Val-Pro-GlyVal-Gly) n , has been considered to be an essential repeated sequence for producing the elastic character of elastin. 1 The previous structural studies have been concentrated to clarify whether the unit, Pro-Gly, in the sequence takes β-turn structure. . However, in general, cyclo-peptides take limited conformations because of the presence of many constraints such as steric constraints and hydrogen bonding formation as well as "cyclic" without the end groups. The extension of the information on the structures of cyclo-peptides to linear peptide with similar sequence should be performed very carefully. Thus, it is better to obtain the information on the torsion angles directly for the linear pentapeptide sequence in the solid state if it is possible.In our previous papers, 5-7 13 C solid state NMR such as especially 2D spin-diffusion solid state NMR under off magic angle spinning (OMAS) coupled with 13 C isotope double labeling of specific residues has been successfully used to determine the torsion angles of the backbone amino acid residues for the silk model peptides, (Ala-Gly) 15 and (Ala-Gly-Gly) 10 in the several solid state forms. Especially, a new structural model of (Ala-Gly) 15 as a model of Bombyx mori silk fibroin before spinning could be proposed. 5 In this paper, we synthesized four kinds of the repeated pentapeptide sequences, (VPGVG) 6 , (VPGV-order to obtain the information on the torsion angles of the backbone of two Val residues (Val 14 and Val 16 ) and one Gly residue (Gly 15 ) using both 2D spin-diffusion NMR under OMAS. Especially, the local conformation of the Gly 15 residue was analyzed in detail from the comparison of the calculated and observed 2D spin-diffusion NMR spectra. EXPERIMENTALThe 13 C-labeled and un-labeled peptides mentioned above were synthesized by the solid-phase method. The samples are purified by HPLC with water and are freeze-dried. The 13 C CP/MAS NMR measurements were performed on a Chemagnetics Infinity 400 MHz spectrometer. A 1 H π/2 pulse of duration 3.0-6.0 µs and a contact time of 1 ms was used. The 2D spin-diffusion NMR spectra were obtained with Varian Unity INOVA 400 NMR spectrometer and 7 mm Jakobsen-type double-tuned MAS probe at off magic angle condition (θ m + 9 • ) and sample spinning of 6 kHz at room temperature. The scaling factor of the 2D spin-diffusion spectra were 1/2 (3 cos 2 (θ m + 9 • ) −1) = −0.206. The mixing time of 2 s was optimized for spin diffusion between intramolecular specific carbon atoms of selectively isotope-labeled Val and Gly residues; however, for no spin-diffusion between intermolecular carbon atoms. [5][6][7] The contact time was set to 2 ms using the Variable-Amplitude CP technique. 8 About 400 scans with a number of t 1 points of 150 and a recy- †

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Section: Methodsmentioning

confidence: 99%

Conformational Characterization of (Val-Pro-Gly-Val-Gly)6 with 13C Solid State NMR

Asakura

Ashida

Ohgo

2003

Polym J

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“…A dominant feature of the tropoelastin amino acid sequence is its well-characterized alternating hydrophobic and hydrophilic domain structure. Hydrophobic regions of tropoelastin feature non-polar amino acids such as glycine, valine, proline and leucine, [3] often arranged in repetitive motifs, the most common being the repeating sequence VGVAPG [4]. Overall, hydrophobic residues account for 82% of the primary sequence [5].…”

Section: Introductionmentioning

confidence: 99%

Tropoelastin: A versatile, bioactive assembly module

et al. 2014

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Elastin provides structural integrity, biological cues and persistent elasticity to a range of important tissues including the vasculature and lungs. Its critical importance to normal physiology makes it a desirable component of biomaterials that seek to repair or replace these tissues. The recent availability of large quantities of the highly purified elastin monomer, tropoelastin, have allowed for a thorough characterization of the mechanical and biological mechanisms underpinning the benefits of mature elastin. While tropoelastin is a flexible molecule, a combination of optical and structural analyses has defined key regions of the molecule that directly contribute to the elastomeric properties and control the cell interactions of the protein. Insights into the structure and behavior of tropoelastin have translated into increasingly sophisticated elastin-like biomaterials, evolving from classically manufactured hydrogels and fibers to new forms, stabilized in the absence of incorporated cross-linkers. Tropoelastin is also compatible with synthetic and natural co-polymers, expanding the applications of its potential use beyond traditional elastin-rich tissues and facilitating finer control of biomaterial properties and the design of next-generation tailored bioactive materials.

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“…The silk‐like unit is prevalent in silk fibroin from Bombyx mori and spontaneously forms hydrogen‐bonded β‐sheets crystals which impart thermal and chemical stability . The elastin‐like unit, on the other hand, is a flexible component which has been reported as displaying a highly flexible conformation . The periodic inclusion of elastomeric sequences in SELPs reduces the overall crystallinity of the system by disrupting the silk‐like blocks and increases its flexibility and aqueous solubility .…”

Section: Introductionmentioning

confidence: 99%

Exploring the Properties of Genetically Engineered Silk‐Elastin‐Like Protein Films

Machado

Costa

Sencadas

et al. 2015

Macromolecular Bioscience

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Free standing films of a genetically engineered silk-elastin-like protein (SELP) were prepared using water and formic acid as solvents. Exposure to methanol-saturated air promoted the formation of aggregated β-strands rendering aqueous insolubility and improved the mechanical properties leading to a 10-fold increase in strain-to-failure. The films were optically clear with resistivity values similar to natural rubber and thermally stable up to 180 °C. Addition of glycerol showed to enhance the flexibility of SELP/glycerol films by interacting with SELP molecules through hydrogen bonding, interpenetrating between the polymer chains and granting more conformational freedom. This detailed characterization provides cues for future and unique applications using SELP based biopolymers.

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Structural investigation of the poly(pentapeptide) of elastin, poly(GVGVP), in the solid state

Cited by 30 publications

References 14 publications

Conformational Characterization of (Val-Pro-Gly-Val-Gly)6 with 13C Solid State NMR

Conformational Characterization of (Val-Pro-Gly-Val-Gly)6 with 13C Solid State NMR

Tropoelastin: A versatile, bioactive assembly module

Exploring the Properties of Genetically Engineered Silk‐Elastin‐Like Protein Films

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