Capillary electromigration methods for the study of collagen

Mikšı́k, Ivan; Sedláková, Pavla; Mikulíková, Kateřina; Eckhardt, Adam

doi:10.1016/j.jchromb.2006.02.043

Cited by 10 publications

(8 citation statements)

References 40 publications

(36 reference statements)

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“…It could be demonstrated by the anisotropic structure of tendon collagen which exhibits high tensile stress in one direction that differs significantly from, e.g., skin collagen made up of loosely connected flexible fibers and cornea collagen consisting of periodic structural layers . The most abundant collagens are those which take the form of fibrils or networks . It is important to note here that the term “collagen” employed in reports is applied in a general sense and may describe individual molecules, native fibrils in situ or in vitro, aggregates or bulk material of an unspecified nature.…”

Section: Collagen—its Structure Composition and Stabilitymentioning

confidence: 99%

“…Hydroxyproline (4‐Hyp) is responsible for the formation of intra‐molecular hydrogen bonds and increases stability of the triple helical domain conformation and integrity of collagen . Previous reports describe a strong linear correlation between the degree of crosslinking and 4‐Hyp content .…”

Section: Collagen—its Structure Composition and Stabilitymentioning

confidence: 99%

“…Owing to the poor solubility qualities of native collagen, it often exhibits a slow metabolic turnover . Water and enzymes contribute to digestion of collagen linkages and its degradation…”

Section: Collagen—its Structure Composition and Stabilitymentioning

confidence: 99%

“…Physiological crosslinks (arising from post‐translational modification of the native collagen) may be divided into two types: enzymatically formed (using lysil oxidase) and nonenzymatic links like advanced glycation end‐products (AGEs) . Frequent causes of pathological networking are oxidative stress, diabetes, and also aging of collagen caused by glycoxidation reaction in the presence of extracellular reducing sugars and free oxygen radicals …”

Section: Crosslinking Of Collagenmentioning

confidence: 99%

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Collagen and Its Modifications-Crucial Aspects with Concern to Its Processing and Analysis

Rýglová

Braun

Suchý

2017

Macromol. Mater. Eng.

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Many connective tissue diseases and defects are associated with poor synthesis or excessive degradation of collagen. The modern tissue engineering approach is to replace the defective site via the implantation of a biocompatible scaffold which serves as a carrier for cell incorporation, proliferation, and growth. Collagen is widely used in the field of clinical medicine in connection with both hard and soft tissue applications. However, certain collagen properties such as poor dimensional stability, poor in vivo mechanical strength, low degree of elasticity, variable nature in terms of enzymatic degradation, crosslinking density, fiber size, trace impurities, and side effects frequently limit both its analysis and application. This review focuses particularly on the processing and modification of collagen type I with respect to its biological and mechanical properties. The processing of collagen into scaffolds is crucial to mimic successfully the extracellular matrices. Moreover, the review suggests several ways in which the most common problems related to the isolation, handling, electrospinning, and crosslinking of collagen can be overcome while maintaining its native character as much as possible. Further, the review provides a summary of the analytical methods available for the physicochemical characterization of collagen with respect to both its molecular and submolecular structure.

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Section: Collagen—its Structure Composition and Stabilitymentioning

confidence: 99%

Section: Collagen—its Structure Composition and Stabilitymentioning

confidence: 99%

“…Owing to the poor solubility qualities of native collagen, it often exhibits a slow metabolic turnover . Water and enzymes contribute to digestion of collagen linkages and its degradation…”

Section: Collagen—its Structure Composition and Stabilitymentioning

confidence: 99%

Section: Crosslinking Of Collagenmentioning

confidence: 99%

See 2 more Smart Citations

Collagen and Its Modifications-Crucial Aspects with Concern to Its Processing and Analysis

Rýglová

Braun

Suchý

2017

Macromol. Mater. Eng.

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“…A citrate-phosphate buffer (25 mmol/L, pH 3.5, 20% ACN) was used. Three types of peptide mixtures were used to evaluate the separation performance of ROMP monoliths: (i) model mixture of nine synthetic oligopeptides, (ii) a tryptic digest of BSA (after pretreatment with dithithreitol and iodoacetic acid) [29] and (iii) a collagenase digest of the collagen type I [30].…”

mentioning

confidence: 99%

Voltage‐assisted capillary LC of peptides using monolithic capillary columns prepared by ring‐opening metathesis polymerization

et al. 2007

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We examined the use of monolithic capillary columns prepared via ring-opening metathesis polymerization (ROMP) for peptide separation in voltage-assisted capillary LC (voltage-assisted CLC). In order to demonstrate their potential for peptide separation, ROMP-derived monoliths with RP properties were prepared. The preparation procedure of monoliths was transferred from ROMP monoliths optimized for CLC. ROMP monoliths were synthesized within the confines of 200 microm id fused-silica capillaries with a length of 37 cm. After optimization of the chromatographic conditions, the separation performance was tested using a well-defined set of artificial peptides as well as two peptidic mixtures resulting from a tryptic digest of BSA as well as a collagenase digest of collagen. ROMP monoliths showed comparable performance to other monolithic separation media in voltage-assisted CLC published so far. Therefore, we conclude that by optimizing the composition of the ROMP monoliths as well as by using the controlled manner of their functionalization, ROMP monoliths bear a great potential in CLC and CEC.

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CEC: A tool for mimicking collagen–surface interactions with apolipoprotein B‐100 peptides

et al. 2009

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Collagens I and III are involved in the formation of the extracellular matrix and presumably in the development of several diseases, such as atherosclerosis. In this study, stable collagen and collagen-decorin coatings were prepared on the inner surfaces of fused silica CEC capillaries, enabling study of the interactions between collagen and selected peptide fragments of apolipoprotein B-100 (apoB-100), the main protein of low-density lipoprotein (LDL) particles. Interactions of positive, neutral, and negative peptide fragments of apoB-100 were elucidated. The selected positive peptide contains the sequence involved in the interaction of LDL with LDL receptor and proteoglycans. Retention factors of the peptides that were determined without any voltage, by exploiting pressure, gave numerical information about interactions with the collagen coatings. The inclusion of decorin in the coatings confirmed the importance of glycosaminoglycans in mediating the interactions between collagens and apoB-100 peptide fragments. The studies support earlier findings that collagens I and III take part in the retention of LDL particles in the intima through binding with a specific positive site on apoB-100. The method developed is simple, but also inexpensive since only small amounts of peptides and collagens are required. Atomic force microscopy images provided valuable information about the topography of collagen and collagen-decorin coatings on the capillary wall.

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Capillary electromigration methods for the study of collagen

Cited by 10 publications

References 40 publications

Collagen and Its Modifications-Crucial Aspects with Concern to Its Processing and Analysis

Collagen and Its Modifications-Crucial Aspects with Concern to Its Processing and Analysis

Voltage‐assisted capillary LC of peptides using monolithic capillary columns prepared by ring‐opening metathesis polymerization

CEC: A tool for mimicking collagen–surface interactions with apolipoprotein B‐100 peptides

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