Effect of NaCl on the Exothermic and Endothermic Components of the Inverse Temperature Transition of a Model Elastin-like Polymer

Reguera, Javier; Urry, Dan W.; Parker, Timothy M.; McPherson, David T.; Rodríguez‐Cabello, José Carlos

doi:10.1021/bm060936l

Cited by 98 publications

(115 citation statements)

References 35 publications

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“…An intriguing characteristic of the pentapeptide (VPGVG) n is that it undergoes coacervation (also termed the inverse temperature transition) over the temperature range of 20°C and 40°C, similar to elastin 9,19–21 . In practice, the inverse temperature transition may be experimentally controlled by the length or arrangement of the repeating motif 22,23 and salt concentration 24–26 . The biomechanically tunable characteristics of elastin-like peptides of VPGVG motifs has led to many intriguing applications, including drug delivery 27,28 .…”

Section: Introductionmentioning

confidence: 99%

Quantitative comparison of structure and dynamics of elastin following three isolation schemes by 13C solid state NMR and MALDI mass spectrometry

Papaioannou

Louis

Dhital

et al. 2015

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Methods for isolating elastin from fat, collagen, and muscle, commonly used in the design of artificial elastin based biomaterials, rely on exposing tissue to harsh pH levels and temperatures that usually denature many proteins. At present, a quantitative measurement of the modifications to elastin following isolation from other extracellular matrix constituents has not been reported. Using magic angle spinning 13C NMR spectroscopy and relaxation methodologies, we have measured the modification in structure and dynamics following three known purification protocols. Our experimental data reveal that the 13C spectra of the hydrated samples appear remarkably similar across the various purification methods. Subtle differences in the half maximum widths were observed in the backbone carbonyl suggesting possible structural heterogeneity across the different methods of purification. Additionally, small differences in the relative signal intensities were observed between purified samples. Lyophilizing the samples results in a reduction of backbone motion and reveals additional differences across the purification methods studied. These differences were most notable in the alanine motifs indicating possible changes in cross-linking or structural rigidity. The measured correlation times of glycine and proline moieties are observed to also vary considerably across the different purification methods, which may be related to peptide bond cleavage. Lastly, the relative concentration of desmosine cross-links in the samples quantified by MALDI mass spectrometry is reported.

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Section: Introductionmentioning

confidence: 99%

Quantitative comparison of structure and dynamics of elastin following three isolation schemes by 13C solid state NMR and MALDI mass spectrometry

Papaioannou

Louis

Dhital

et al. 2015

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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“…Increasing the ionic strength of an ELR solution also influences the T t and is particularly useful to trigger the ITT phenomenon when its concentration is low. Reguera et al [95] suggested that an increase in the salt concentration increases the polarity of the solvent. This creates a higher difference in polarity with respect to the hydrophobic moieties of the polymer, recruiting more and more ordered water molecules to surround the polymer chains.…”

Section: General Properties Of Elastin-like Recombinamersmentioning

confidence: 99%

Elastin‐Like Macromolecules

Costa

Martin

Mano

et al. 2012

Biomimetic Approaches for Biomaterials Development

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“…This effect is well reported in the literature although those studies were mainly a quantification of the phenomenon. [36,37] More recently, Reguera et al, [38] making use of temperature-modulated DSC, have proposed a more detailed explanation. According to that work, the increase in DH, and the concurrent decrease in T t , appears both in the enthalpy related with the folding of the polymer and in the contribution associated with disruption of the structured water of hydrophobic hydration.…”

Section: Production and Stimuli-responsive Behavior Of H-rgd6mentioning

confidence: 99%

Stimuli‐Responsive Thin Coatings Using Elastin‐Like Polymers for Biomedical Applications

Costa

Custódio

Testera

et al. 2009

Adv Funct Materials

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Smart thin coatings using a recombinant elastin‐like polymer (ELP) containing the cell attachment sequence arginine–glycine–(aspartic acid) (RGD) are fabricated for the first time through simple deposition of the ELP dissolved in aqueous‐based solutions. The biopolymer is produced and characterized using electrophoresis and mass spectroscopy. The temperature and pH responsiveness are assessed by aggregate size measurements and differential scanning calorimetry. The deposition of the studied ELP onto chitosan is followed in situ with a quartz‐crystal microbalance with dissipation monitoring (QCM‐D). Contact angle measurements are performed at room temperature and at 50 °C, showing reversible changes from a moderate hydrophobic behavior to an extremely wettable surface. AFM analysis performed at room temperature reveals a smooth surface and no organized structure. At 50 °C, the surface presents spherical nanometer‐sized structures of collapsed biopolymer chains. Such results suggest that the ELP chains, when collapsed, aggregate into micelle‐like structures at the surface of the substrate, increasing its water affinity. Cell adhesion tests on the developed coatings are conducted using a SaOS‐2 cell line. Enhanced cell adhesion could be observed in the H‐RGD6‐coated surfaces, as compared with the original chitosan monolayer. An intermediate behavior is found in chitosan coated with the corresponding ELP without the RGD sequence. Therefore, the developed films have great potential as biomimetic coatings of biomaterials for different biomedical applications, including tissue engineering and controlled delivery of bioactive agents. Their thermo‐responsive behavior can also be exploited for tunable cell adhesion and controlled protein adsorption.

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Effect of NaCl on the Exothermic and Endothermic Components of the Inverse Temperature Transition of a Model Elastin-like Polymer

Cited by 98 publications

References 35 publications

Quantitative comparison of structure and dynamics of elastin following three isolation schemes by 13C solid state NMR and MALDI mass spectrometry

Quantitative comparison of structure and dynamics of elastin following three isolation schemes by 13C solid state NMR and MALDI mass spectrometry

Elastin‐Like Macromolecules

Stimuli‐Responsive Thin Coatings Using Elastin‐Like Polymers for Biomedical Applications

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