Normal Thermal Stability of an Overmodified Type I Collagen Despite a Structural Mutation within the Triple Helical Region in a Case of Osteogenesis Irnperfecta Type IVB

1988 ◽  
Vol 543 (1 Third Interna) ◽  
pp. 83-84 ◽  
Author(s):  
P. M. ROYCE ◽  
A. SUPERTI-FURGA ◽  
V. H. RAO ◽  
B. STEINMANN
Keyword(s):  
Thermal Stability ◽  
Type I Collagen ◽  
Type I ◽  
Structural Mutation ◽  
Thermal Stability Of ◽  
Helical Region

scholarly journals Thermal stability of human-fibroblast-collagenase-cleavage products of type-I and type-III collagens

1987 ◽  
Vol 247 (3) ◽  
pp. 725-729 ◽  
Author(s):  
C C Danielsen
Keyword(s):  
Thermal Stability ◽  
Human Fibroblast ◽  
Type I Collagen ◽  
Type Iii Collagen ◽  
Type I ◽  
Type Iii ◽  
Melting Temperatures ◽  
Large Type ◽  
Fibroblast Collagenase ◽  
Thermal Stability Of

Rat skin type-I and type-III collagens were degraded by human fibroblast collagenase at a temperature below the ‘melting’ temperature for the two resulting fragments, namely the N-terminal three-fourths, TCA, and the C-terminal one-fourth, TCB. The specific cleavage of the collagen was confirmed by electrophoresis and determination of molecular length by electron microscopy. The two fragments were separated by gel filtration and the thermal stabilities of the isolated fragments were determined. For type-I collagen, the ‘melting’ temperatures of the two fragments were found to differ by only 0.5 degrees C and were 4.5-5.0 degrees C below that of the uncleaved molecule. The ‘melting’ temperatures of the uncleaved molecule and the N-terminal fragment were independent of the extent of N-terminal intramolecular cross-linking. For type-III collagen, the ‘melting’ temperatures of the fragments were found to differ by 1.3 degrees C. The small fragments of the two types of collagen ‘melted’ at the same temperature, whereas the large type-III fragment ‘melted’ at a slightly higher temperature than did the large type-I fragment. Reduction of the disulphide bonds located in the C-terminal type-III fragment did not affect the thermal stability of this fragment. The thermal stability of uncleaved type-III collagen was found to be variable, but the reason for this is not known at present.

Thermal Properties of Mineralized and Non Mineralized Type I Collagen in Bone

2002 ◽  
Vol 724 ◽  
Author(s):  
L. F. Lozano ◽  
M. A. Peña-Rico ◽  
H. Jang-Cho ◽  
A. Heredia ◽  
E. Villarreal ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Type I Collagen ◽  
Combustion Process ◽  
Stability Loss ◽  
Human Bone ◽  
Type I ◽  
Global Effect ◽  
Cross Links ◽  
The Stability ◽  
Thermal Stability Of

AbstractThe research about the structural stability of bone, as a composite material, compromises a complete understanding of the interaction between the mineral and organic phases. The thermal stability of human bone and type I collagen extracted from human bone by different methods was studied in order to understand the interactions between the mineral and organic phases when is affected by a degradation/combustion process. The experimental techniques employed were calorimetry and infrared spectroscopy (FTIR) techniques. The extracted type I collagens result to have a bigger thermal stability with a Tmax at 500 and 530 Celsius degrees compared with the collagen present in bone with Tmax at 350 Celsius degrees. The enthalpy value for the complete degradation/combustion process were similar for all the samples, being 8.4 +- 0.11 kJ/g for recent bones diminishing with the antiquity, while for extracted collagens were 8.9 +- 0.07 and 7.9 +-1.01 kJ/g. These findings demonstrate that the stability loss of type I collagen is due to its interactions with the mineral phase, namely carbonate hydroxyapatite. This cause a change in the molecular properties of the collagen during mineralization, specifically in its cross-links and other chemical interactions, which have a global effect over the fibers elasticity, but gaining tensile strength in bone as a whole tissue. We are applying this characterization to analyze the diagenetic process of bones with archaeological interest in order to identify how the environmental factors affect the molecular structure of type I collagen. In bone samples that proceed from an specific region with the same environmental conditions, the enthalpy value per unit mass was found to diminish exponentially with respect to the bone antiquity.

scholarly journals Embryonic avian cornea contains layers of collagen with greater than average stability.

1986 ◽  
Vol 103 (4) ◽  
pp. 1587-1593 ◽  
Author(s):  
T F Linsenmayer ◽  
E Gibney ◽  
J M Fitch
Keyword(s):  
Thermal Stability ◽  
Type I Collagen ◽  
Collagen Fibrils ◽  
Collagen Molecule ◽  
Type I ◽  
Corneal Tissue ◽  
Tissue Sections ◽  
Triple Helical Domain ◽  
Thermal Stability Of

A unique morphological feature of the embryonic avian cornea is the uniformity of its complement of striated collagen fibrils, each of which has a diameter of 25 nm. We have asked whether this apparent morphological uniformity also reflects an inherent uniformity of the structural and physical properties of these fibrils. For this we have examined the in situ thermal stability of the type I collagen within these fibrils. Corneal tissue sections were reacted at progressively higher temperatures with conformation-dependent monoclonal antibodies directed against the triple-helical domain of the type I collagen molecule. These studies show that the cornea contains layers of collagen fibrils with greater than average stability. The two most prominent of these extend uninterrupted across the entire width of the cornea, and then appear to insert into thick bundles of scleral collagen, which in turn appear to insert into the scleral ossicles, a ring of bony plates which circumscribe the sclera of the avian eye. Once formed, the bands may act to stabilize the shape of the cornea or, conversely, to alter it during accommodation.

scholarly journals Difference in thermal stability of type-I and type-III collagen from rat skin

1982 ◽  
Vol 203 (1) ◽  
pp. 323-326 ◽  
Author(s):  
Carl Christian Danielsen
Keyword(s):  
Thermal Stability ◽  
Type I Collagen ◽  
Type Iii Collagen ◽  
Type I ◽  
Neutral Salt ◽  
Rat Skin ◽  
Thermal Stabilities ◽  
Type Iii ◽  
Thermal Stability Of ◽  
Salt Fractionation

Type-I and type-III collagens were obtained by differential salt fractionation of neutral-salt-soluble collagen from rat skin. Their thermal stabilities were determined by u.v. difference spectroscopy. The ‘melting’ temperature (Tm) in 5mm-acetic acid of type-III collagen was almost 2°C above that of type-I collagen. Intramolecular covalent cross-linking had no effect on the thermal stability.

scholarly journals Molecular simulations reveal that a short helical loop regulates thermal stability of type I cohesin–dockerin complexes

2018 ◽  
Vol 20 (45) ◽  
pp. 28445-28451 ◽  
Author(s):  
Melissabye Gunnoo ◽  
Pierre-André Cazade ◽  
Edward A. Bayer ◽  
Damien Thompson
Keyword(s):  
Thermal Stability ◽  
Protein Complexes ◽  
Molecular Simulations ◽  
Type I ◽  
Thermal Stability Of

Re-engineering linker regions to boost the thermal stability of protein–protein complexes.

scholarly journals Swim bladder collagen forms hydrogel with macroscopic superstructure by diffusion induced fast gelation

2015 ◽  
Vol 3 (39) ◽  
pp. 7658-7666 ◽  
Author(s):  
Md. Tariful Islam Mredha ◽  
Xi Zhang ◽  
Takayuki Nonoyama ◽  
Tasuku Nakajima ◽  
Takayuki Kurokawa ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Type I Collagen ◽  
Type I ◽  
Swim Bladder ◽  
P Type

Type I collagen extracted from the swim bladder of Bester sturgeon forms an oriented hydrogel with mechanical and thermal stability by diffusion induced fast gelation.

scholarly journals The chemistry of the collagen cross-links. Purification and characterization of cross-linked polymeric peptide material from mature collagen containing unknown amino acids

1980 ◽  
Vol 185 (2) ◽  
pp. 373-381 ◽  
Author(s):  
N D Light ◽  
A J Bailey
Keyword(s):  
Amino Acids ◽  
Type I Collagen ◽  
Gel Filtration ◽  
Amino Acid Content ◽  
Exchange Chromatography ◽  
Type I ◽  
Polymeric Form ◽  
Cross Links ◽  
Helical Region

A polymeric form of the alpha 1-chain C-terminal peptide alpha 1 CB6 (poly-alpha 1 CB6) was purified from CNBr digests of insoluble bovine tendon type-I-collagen by gel filtration and ion-exchage chromatography. The purified material had a molecular weight of 1.5 × 10(6)-5 × 10(6) on gel filtration and an amino acid content virtually identical with that of monomeric peptide alpha 1 CB6. The material could be adsorbed on affinity gels containing immobilized anti-(alpha 1 CB6-peptide non-helical region) antibodies and was an inhibitor of haemagglutination by the same antibodies of alpha 1 CB6-peptide-coated sheep erythrocytes. Periodate treatment of the material had no effect. Alkali hydrolysates were shown to contain two unknown amino acids, which were purified by gel filtration and ion-exchange chromatography in volatile buffers and are believed to be components of the mature cross-link of collagen.

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