Structural properties of pepsin-solubilized collagen acylated by lauroyl chloride along with succinic anhydride

Li, Conghu; Tian, Zhenhua; Liu, Wentao; Li, Guoying

doi:10.1016/j.msec.2015.05.055

Cited by 20 publications

(9 citation statements)

References 41 publications

(51 reference statements)

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“…Indeed, the fact that it is soluble in weakly acid solutions, while aggregating and precipitating at physiological values of pH, drastically limits its use for the formulation of hydrogels or injectable suspensions. Some manufacturing "tricks" were developed in order to make native-like ultrastructured insoluble collagen soluble at neutral pH (Li et al, 2015;Zhang M. et al, 2018;Yang et al, 2020a,b). Among these, acylation and desamidation were set up to induce shifts of the collagen isoelectric point to lower values.…”

Section: Impact On Supramolecular Structurementioning

confidence: 99%

Mimicking the Hierarchical Organization of Natural Collagen: Toward the Development of Ideal Scaffolding Material for Tissue Regeneration

Salvatore

Gallo

Natali

et al. 2021

Front. Bioeng. Biotechnol.

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Biological materials found in living organisms, many of which are proteins, feature a complex hierarchical organization. Type I collagen, a fibrous structural protein ubiquitous in the mammalian body, provides a striking example of such a hierarchical material, with peculiar architectural features ranging from the amino acid sequence at the nanoscale (primary structure) up to the assembly of fibrils (quaternary structure) and fibers, with lengths of the order of microns. Collagen plays a dominant role in maintaining the biological and structural integrity of various tissues and organs, such as bone, skin, tendons, blood vessels, and cartilage. Thus, “artificial” collagen-based fibrous assemblies, endowed with appropriate structural properties, represent ideal substrates for the development of devices for tissue engineering applications. In recent years, with the ultimate goal of developing three-dimensional scaffolds with optimal bioactivity able to promote both regeneration and functional recovery of a damaged tissue, numerous studies focused on the capability to finely modulate the scaffold architecture at the microscale and the nanoscale in order to closely mimic the hierarchical features of the extracellular matrix and, in particular, the natural patterning of collagen. All of these studies clearly show that the accurate characterization of the collagen structure at the submolecular and supramolecular levels is pivotal to the understanding of the relationships between the nanostructural/microstructural properties of the fabricated scaffold and its macroscopic performance. Several studies also demonstrate that the selected processing, including any crosslinking and/or sterilization treatments, can strongly affect the architecture of collagen at various length scales. The aim of this review is to highlight the most recent findings on the development of collagen-based scaffolds with optimized properties for tissue engineering. The optimization of the scaffolds is particularly related to the modulation of the collagen architecture, which, in turn, impacts on the achieved bioactivity.

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Section: Impact On Supramolecular Structurementioning

confidence: 99%

Mimicking the Hierarchical Organization of Natural Collagen: Toward the Development of Ideal Scaffolding Material for Tissue Regeneration

Salvatore

Gallo

Natali

et al. 2021

Front. Bioeng. Biotechnol.

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“…28,29 In our previous report, the acylated collagen had tyrosine and phenylalanine residues, suggesting that the acylated collagen could exhibit fluorescent property. 22 However, the quantum yields of tyrosine (0.14) are about five times than that of phenylalanine, 14 demonstrating that the intrinsic fluorescence of the native or acylated collagens might mainly come from tyrosine. Therefore, we carried out the fluorescence measurements at the maximum excitation wavelength of 275 nm for better understanding the aggregation behavior of the acylated collagen.…”

Section: Fluorescence Measurements Of the Acylated And The Native Colmentioning

confidence: 99%

“…In previous works, a new kind of hydrophobic acylated collagen was prepared, 21–23 which might be used in the dispersion and the sustained release for hydrophobic drugs. 24 Since the hydrophobicity of the acylated collagen was enhanced, the aggregation behavior of the acylated collagen in solution might be changed at different conditions.…”

Section: Introductionmentioning

confidence: 99%

“…18,19 For instance, Ding et al found that the band at 283 nm changed before that at 288 nm when the temperature of collagen solution was lower than 32 C since both the signs of c(283, 288) and È(283, 288) were positive. 13 As determined using 2D correlation spectra, Wu et al found that the hydrogen bonds between the tyrosine residues in the collagen molecules formed when the temperature was lower than 30 C. 20 In previous works, a new kind of hydrophobic acylated collagen was prepared, [21][22][23] which might be used in the dispersion and the sustained release for hydrophobic drugs. 24 Since the hydrophobicity of the acylated collagen was enhanced, the aggregation behavior of the acylated collagen in solution might be changed at different conditions.…”

Section: Introductionmentioning

confidence: 99%

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Aggregation Behavior of Acylated Pepsin-Solubilized Collagen Based on Fluorescence Spectrum Technology

et al. 2020

Appl Spectrosc

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The aggregation behavior of collagen-based materials plays an important role in their processing because it could affect their physicochemical properties. Based on the intrinsic fluorescence characteristic of tyrosine, fluorescence spectrum technology was used to investigate the aggregation state of the acylated collagen molecules in aqueous solution. The results showed that the aggregate degree of the acylated collagen was higher than that of the native collagen due to the hydrophobic interaction. With the increase of concentrations of the acylated collagen or at NaCl higher than 40 mmol/L, the aggregate degree of the acylated collagen molecules increased. When the pH was close to the isoelectric point of the acylated collagen, the hydrophobic interaction and the hydrogen bond helped to increase the aggregation degree. However, with the increase of temperature (10–70 ℃), the aggregation state of the acylated collagen decreased gradually due to the quenching, the molecular collision, and the broken of hydrogen bonds. Furthermore, two-dimensional correlation spectroscopy (2D-COS) showed that the response order was 360 > 305 nm at various acylated collagen and NaCl (>40 mmol/L) concentrations, while the response order was 305 > 360 nm when the pH value was increased from 5.0 to 9.0. Temperature-dependent 2D-COS showed there were four bands that occurred and the response order was listed as follows: 293 > 305 > 360 > 420 nm. In brief, the results might provide an important guide for molding processes of the acylated collagen.

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“…Para el caso de los recubrimientos con adiciones de colágeno (condiciones II y III) se identifican varios solapes, como por ejemplo a 1652 cm -1 para la Amida I y a 1552 cm -1 para la Amida II entre los enlaces del quitosano y el colágeno, como también a 1240 cm -1 y 1238 cm -1 los solapes entre los enlaces de la policaprolactona estiramiento COC asimétrico y del colágeno la Amida III estiramiento N-H y CH 2 de la glicina [20] . Por otra parte los contrastes de color claros a oscuros en unas zonas más que en otras de la figura 5 c) sugieren la deposición del colágeno de manera discontinua [21] y se ha relacionado con la presencia elemental de más carbono y oxígeno [22] .…”

Section: Caracterización Composicional De Los Recubrimientos Poliméricosunclassified

Morphological and electrochemical behavior of polycaprolactone-chitosan-collagen film fabricated by Dip Coating on Ti6Al4V

Rueda

Ballesteros

Durán

2017

Rev. Mex. Ing. Biomed.

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la aleación Ti6Al4V recubierta por las mezclas de polímeros a cero días de inmersión en Fluido Corporal Simulado y la capacidad de adsorción de calcio a 21 días de inmersión. De esta manera, se encontraron efectos representativos sobre el papel del colágeno para el aumento de la rugosidad superficial, mayores valores en la resistencia a la polarización del Ti6Al4V, mejor comportamiento en los parámetros de energía libre, adsorción atómica de calcio y la consolidación de una nueva interfase asociada a la monocapa de calcio simulada mediante circuitos equivalentes y observada por Microscopía Electrónica de Barrido.

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Structural properties of pepsin-solubilized collagen acylated by lauroyl chloride along with succinic anhydride

Cited by 20 publications

References 41 publications

Mimicking the Hierarchical Organization of Natural Collagen: Toward the Development of Ideal Scaffolding Material for Tissue Regeneration

Mimicking the Hierarchical Organization of Natural Collagen: Toward the Development of Ideal Scaffolding Material for Tissue Regeneration

Aggregation Behavior of Acylated Pepsin-Solubilized Collagen Based on Fluorescence Spectrum Technology

Morphological and electrochemical behavior of polycaprolactone-chitosan-collagen film fabricated by Dip Coating on Ti6Al4V

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