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Interaction of bilirubin with reconstituted collagen fibrils.

ABSTRACT: 1. Interaction of bilirubin with collagen fibrils was explored in a two-phase system where collagen was present as an opaque rigid gel composed of striated fibrils, and bilirubin as an aqueous solution. 2. The Ka value of the binding of bilirubin to collagen fibrils is 5.4 X 10(3)M-1. The interaction of bilirubin with collagen fibrils depends on temperature. Below 5 degrees C, the binding is greatly diminished and denaturation of collagen fibril aggregates at 52--53 degrees C into a dissolution state abolishes binding of bilirubin. 3. Salicylate and sulphanilamide do not affect the binding of bilirubin to reconstituted collagen fibrils. 4. Serum albumin (40--80mM), known to reverse the binding of bilirubin to lipids, dissociates only 50% of the bilirubin bound to collagen fibrils. This suggests that sites located on collagen participate in some tight binding of bilirubin and the corresponding binding sites on albumin do not compete with them. 5. Urea (4M) abolishes more than 70% of the binding of bilirubin to collagen. Urea and thermal denaturation studies indicate the importance of conformation and organization of collagen fibrillar aggregates for the binding of bilirubin.

SUBMITTER: Kapoor CL

PROVIDER: S-EPMC1165431 | biostudies-other | 1975 May

REPOSITORIES: biostudies-other

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Reconstituted collagen fibrils. Fibrillar and molecular stability of the collagen upon maturation in vitro.

Project description:During the maturation in vitro of reconstituted collagen fibrils prepared from rat skin, the mechanical and thermal stability of collagen increased and the pepsin-solubility decreased. At the same time a larger fraction of the pepsin-soluble collagen attained a lower molecular thermal stability that resulted in a biphasic thermal transition of the soluble collagen. Type-I collagen, with a similar biphasic thermal transition, was isolated from acid-insoluble rat skin collagen.

| S-EPMC1144228 | biostudies-other

Mechanical strain stabilizes reconstituted collagen fibrils against enzymatic degradation by mammalian collagenase matrix metalloproteinase 8 (MMP-8).

Project description:Collagen, a triple-helical, self-organizing protein, is the predominant structural protein in mammals. It is found in bone, ligament, tendon, cartilage, intervertebral disc, skin, blood vessel, and cornea. We have recently postulated that fibrillar collagens (and their complementary enzymes) comprise the basis of a smart structural system which appears to support the retention of molecules in fibrils which are under tensile mechanical strain. The theory suggests that the mechanisms which drive the preferential accumulation of collagen in loaded tissue operate at the molecular level and are not solely cell-driven. The concept reduces control of matrix morphology to an interaction between molecules and the most relevant, physical, and persistent signal: mechanical strain.The investigation was carried out in an environmentally-controlled microbioreactor in which reconstituted type I collagen micronetworks were gently strained between micropipettes. The strained micronetworks were exposed to active matrix metalloproteinase 8 (MMP-8) and relative degradation rates for loaded and unloaded fibrils were tracked simultaneously using label-free differential interference contrast (DIC) imaging. It was found that applied tensile mechanical strain significantly increased degradation time of loaded fibrils compared to unloaded, paired controls. In many cases, strained fibrils were detectable long after unstrained fibrils were degraded.In this investigation we demonstrate for the first time that applied mechanical strain preferentially preserves collagen fibrils in the presence of a physiologically-important mammalian enzyme: MMP-8. These results have the potential to contribute to our understanding of many collagen matrix phenomena including development, adaptation, remodeling and disease. Additionally, tissue engineering could benefit from the ability to sculpt desired structures from physiologically compatible and mutable collagen.

| S-EPMC2925882 | biostudies-literature

Nature designs tough collagen: explaining the nanostructure of collagen fibrils.

Project description:Collagen is a protein material with superior mechanical properties. It consists of collagen fibrils composed of a staggered array of ultra-long tropocollagen (TC) molecules. Theoretical and molecular modeling suggests that this natural design of collagen fibrils maximizes the strength and provides large energy dissipation during deformation, thus creating a tough and robust material. We find that the mechanics of collagen fibrils can be understood quantitatively in terms of two critical molecular length scales chi(S) and chi(R) that characterize when (i) deformation changes from homogeneous intermolecular shear to propagation of slip pulses and when (ii) covalent bonds within TC molecules begin to fracture, leading to brittle-like failure. The ratio chi(S)/chi(R) indicates which mechanism dominates deformation. Our modeling rigorously links the chemical properties of individual TC molecules to the macroscopic mechanical response of fibrils. The results help to explain why collagen fibers found in nature consist of TC molecules with lengths in the proximity of 300 nm and advance the understanding how collagen diseases that change intermolecular adhesion properties influence mechanical properties.

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Structural and Functional Plasticity of Collagen Fibrils.

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| S-EPMC6477584 | biostudies-literature

Molecular mechanics of mineralized collagen fibrils in bone.

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Degradation and Remodeling of Epitaxially Grown Collagen Fibrils.

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| S-EPMC6472930 | biostudies-literature

Deformation micromechanisms of collagen fibrils under uniaxial tension.

Project description:Collagen, an essential building block of connective tissues, possesses useful mechanical properties due to its hierarchical structure. However, little is known about the mechanical properties of collagen fibril, an intermediate structure between the collagen molecule and connective tissue. Here, we report the results of systematic molecular dynamics simulations to probe the mechanical response of initially unflawed finite size collagen fibrils subjected to uniaxial tension. The observed deformation mechanisms, associated with rupture and sliding of tropocollagen molecules, are strongly influenced by fibril length, width and cross-linking density. Fibrils containing more than approximately 10 molecules along their length and across their width behave as representative volume elements and exhibit brittle fracture. Shorter fibrils experience a more graceful ductile-like failure. An analytical model is constructed and the results of the molecular modelling are used to find curve-fitted expressions for yield stress, yield strain and fracture strain as functions of fibril structural parameters. Our results for the first time elucidate the size dependence of mechanical failure properties of collagen fibrils. The associated molecular deformation mechanisms allow the full power of traditional material and structural engineering theory to be applied to our understanding of the normal and pathological mechanical behaviours of collagenous tissues under load.

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Surface-sensitive Raman spectroscopy of collagen I fibrils.

Project description:Collagen fibrils are the main constituent of the extracellular matrix surrounding eukaryotic cells. Although the assembly and structure of collagen fibrils is well characterized, very little appears to be known about one of the key determinants of their biological function-namely, the physico-chemical properties of their surface. One way to obtain surface-sensitive structural and chemical data is to take advantage of the near-field nature of surface- and tip-enhanced Raman spectroscopy. Using Ag and Au nanoparticles bound to Collagen type-I fibrils, as well as tips coated with a thin layer of Ag, we obtained Raman spectra characteristic to the first layer of collagen molecules at the surface of the fibrils. The most frequent Raman peaks were attributed to aromatic residues such as phenylalanine and tyrosine. In several instances, we also observed Amide I bands with a full width at half-maximum of 10-30 cm(-1). The assignment of these Amide I band positions suggests the presence of 3(10)-helices as well as α- and β-sheets at the fibril's surface.

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Preparation of mineralized nanofibers: collagen fibrils containing calcium phosphate.

Project description:We report a straightforward, bottom-up, scalable process for preparing mineralized nanofibers. Our procedure is based on flowing feed solution, containing both inorganic cations and polymeric molecules, through a nanoporous membrane into a receiver solution with anions, which leads to the formation of mineralized nanofibers at the exit of the pores. With this strategy, we were able to achieve size control of the nanofiber diameters. We illustrate this approach by producing collagen fibrils with calcium phosphate incorporated inside the fibrils. This structure, which resembles the basic constituent of bones, assembles itself without the addition of noncollagenous proteins or their polymeric substitutes. Rheological experiments demonstrated that the stiffness of gels derived from these fibrils is enhanced by mineralization. Growth experiments of human adipose derived stem cells on these gels showed the compatibility of the fibrils in a tissue-regeneration context.

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