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Collagen and keratin colloid systems with a multifunctional effect for cosmetic and technical applications / Ján Matyasovsky in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CIX, N° 9 (09/2014)
[article]
Titre : Collagen and keratin colloid systems with a multifunctional effect for cosmetic and technical applications Type de document : texte imprimé Auteurs : Ján Matyasovsky, Auteur ; Ján Sedliacik, Auteur ; Peter Jurkovic, Auteur ; Peter Duchovic, Auteur Année de publication : 2014 Article en page(s) : p. 284-295 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Antimicrobiens
Argent
Barrière cutanée
Biopolymères
Collagène
Colloides
Cosmétiques
Dispersions et suspensions
Emulsions -- Emploi en cosmétologie
Hydratation
Hydrolysats de protéines
kératineLa kératine est une protéine, synthétisée et utilisée par de nombreux êtres vivants comme élément de structure, et également l'exemple-type de protéine fibreuse.
La kératine est insoluble, et peut être retrouvée sur l'épiderme de certains animaux, notamment les mammifères, ce qui leur garantit une peau imperméable. Parfois, lors d'une friction trop importante, la kératine se développe à la surface de la peau formant une callosité. Les cellules qui produisent la kératine meurent et sont remplacées continuellement. Les morceaux de kératine qui restent emprisonnés dans les cheveux sont couramment appelés des pellicules.
La molécule de kératine est hélicoïdale et fibreuse, elle s'enroule autour d'autres molécules de kératine pour former des filaments intermédiaires. Ces protéines contiennent un haut taux d'acides aminés à base de soufre, principalement la cystéine, qui forment un pont disulfure entre les molécules, conférant sa rigidité à l'ensemble. La chevelure humaine est constituée à 14 % de cystéine.
Il y a deux principales formes de kératines : l'alpha-kératine, ou α-keratin, présente chez les mammifères notamment, dont l'humain, et la bêta-kératine, ou β-keratin, que l'on retrouve chez les reptiles et les oiseaux. Ces deux types de kératines ne présentent clairement pas d'homologie de séquence.
Chez l'être humain, la kératine est fabriquée par les kératinocytes, cellules se trouvant dans la couche profonde de l'épiderme. Les kératinocytes absorbent la mélanine (pigment fabriqué par les mélanocytes), se colorent et ainsi cette pigmentation de l'épiderme permet de protéger les kératinocytes des rayons ultraviolets du Soleil.
Liposomes
Peau -- Soins et hygiène
Produits antisolaires
Produits hydratants
Taille des particules
Tension superficielle
ViscositéIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : Fibril proteins of leather, mainly collagen, keratin, glycoproteins, hetero-polysaccharides as hyaluronic acid are the most significant from the view of application in cosmetics. Collagen is the most widespread animal protein component of skin, tendon, bones and ligament. Keratin is the main component of hair, fur, feathers, hooves, horns and outer surface of the skin. Keratin is characterized by a high content of sulfur amino acid cysteine with a typical formation of disulfide bridges. Modified collagen is the basis for several types of test colloids, where agents for the regeneration of the skin, with a high degree of its hydration appear very promising. Originality of the research was ensured as well by the biopolymer keratin as natural anti-solar protection of skin. This knowledge is based on physiological presence of keratinocytes in leather and connected protective mechanism against the effects of the sun. The aim of this work was to develop liposome colloid systems based on biopolymers with a multifunctional effect and to obtain higher benefit of cosmetic preparations e.g. increased hydration, regeneration, protection against ultraviolet radiation, barrier protection of the skin etc. and to ensure microbiologic stability of these systems by the application of colloid silver. Samples of biopolymers, dispersions, emulsions and liposomes were evaluated by the determination of their basic qualitative parameters as viscosity, dry content matter, size of particles and stability. Hydrolysates of keratin lower surface tension from the value ã = 72.8 mN.m-1 to the value approx. ã = 55.5 mN.m-1, and therefore, research was oriented to the possibility of lower dosing of synthetic emulsifier at keeping of required stability of hydrogels and hydro-creams. Results of testing samples confirmed increased hydration of the skin and protection mainly against UVB radiation. Evaluation of disinfectant efficiency of prepared colloidal silver confirmed the bactericidal, fungicidal and sporocidal effect against a broad spectrum of bacteria, fungi and microbes. Note de contenu : - Notation and description of samples
- Assessment of medium molecular weights
- Assessment of tatal and bonded sulfur in samples
- Stalagmometric method for measuring surface tension of water, collagen and keratin
- Applicative verification of effects of biopolymers
- Testing of hydration and protection effects on the skin
- Investigation of the dermal effect of modified colloidal systems on the skin
- Investigation of the biocide effect of modified colloidal systems by silver on the skin
- Modification of collagen by colloidal silverEn ligne : https://drive.google.com/file/d/16tK9Vkusw-mooFPXzYTpTSiFT8qh3NSA/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=21866
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. CIX, N° 9 (09/2014) . - p. 284-295[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 16485 - Périodique Bibliothèque principale Documentaires Disponible Collagen modification using nanotechnologies : a review / Deng-Ge Gao in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CVIII, N° 10 (10/2013)
[article]
Titre : Collagen modification using nanotechnologies : a review Type de document : texte imprimé Auteurs : Deng-Ge Gao, Auteur ; Jian-Zhong Ma, Auteur ; Bin Lv, Auteur ; Zhang Jing, Auteur Année de publication : 2013 Article en page(s) : p. 392-400 Note générale : Bibliogr. Langues : Américain (ame) Catégories : Argent
Argile
Collagène
Copolymères greffés
Copolymérisation
Dioxyde de silicium
Nanoémulsions
Nanoparticules
NanotechnologieIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : The essence of leather the industry is modified collagen fibers. With more challenges facing traditional chemicals used for leather making, along with the development of higher living standards, great demand is imposed on the leather industry. Therefore, more researchers are paying attention to collagen modification using nanotechnologies for the leather industry. In this review, we present a critical discussion of collagen modified by nano-size emulsion, clay minerals, nano silicon dioxide, or nanosilver. In the end, we conclude this review with some perspectives on the future research and development of collagen modified by nanotechnology. Note de contenu : - NANO-SIZE EMULSIONS
- CLAY MINERALS
- NANO SILICON DIOXIDE : Producing nano-Sio2 between fibers on hide by in-situ method - Graft-copolymerization method - Nano dichromium trioxide
- NANOSILVEREn ligne : https://drive.google.com/file/d/18ISw97m7cbVhsuxVWu5B63AbNLO5vYm7/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=19462
in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA) > Vol. CVIII, N° 10 (10/2013) . - p. 392-400[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 15578 - Périodique Bibliothèque principale Documentaires Disponible Collagen : a not so simple protein / A. J. Bailey in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 82, N° 3 (05-06/1998)
[article]
Titre : Collagen : a not so simple protein Type de document : texte imprimé Auteurs : A. J. Bailey, Auteur ; R. G. Paul, Auteur Année de publication : 1998 Article en page(s) : p. 104-110 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Collagène
Cuirs et peauxIndex. décimale : 675 Technologie du cuir et de la fourrure Résumé : Collagen is the major protein of animal bodies from simple sponges to homo sapiens and exists in various froms from skin, tendon and bone to cornea and basement membrane of the capillaries. This biological variation can now be accounted for on the basis of a whole family of genetically distinct collagens. OVer the past two decades 19 different collagens have been identified, although the major types are the fibrous types I, II and III and the non-fibrous type IV of basement membrane. They all possess the basic triple helix based on multiple repeats of the simple tri-peptide Gly-W-Y, but this varies in length and forms different supramolecular aggregates to achieve optimum function for particular tissues. The major function of collagenis to provide shape and mechanical strength and the latter is achieved by intermolecular crosslinking of the collagen molecules in the supramolecular aggreate. The monomeric molecules in the aggregates are stabilised by two different pathways. Initially cross-linking occurs through an enzymic mechanism involving oxidation of specific lysine and hydroxylysine residues providing divalent cross-linking which subsequently matures to multivalent cross-links. As the rate of turnover decreases a non-enzymic pathway takes over, which is mediated throug the adventitious accretion of glucose. Collagen therefore, unlike other proteins shows considerable changes with age which in turn affect its physical properties. These changes must be taker into accoung when preparing collagen based products ?
All the amino acid side chains project radially for the rod-like triple helix and the quarter-staggered array of the molecules allows highly specific intermolecular cross-linking either naturally, or artificially with bifunctional reagents. Reactions with basic or acid groups can therefore be carefully controlled and in some case their location predicted. Synthetic cross-links bind the molecules closer together and increase intermolecular interactions, thus increasing the shrinkage temerature and resistance to enzymic degradation.
The turnover of collagen is generally slow but in fact can vary from 2/3 days for periodontal ligament to several years for skin and tendon. Mature collagen fibres arehighly resistant to enzymes and degradation is achieved by specific collagenase that can cleave the triplehelix at one particular point. The shorter helical fragments can then unravel and denature to gelatin when ogher metalloproteinases (MMPs) degrade it to amino acids. A family of 14 metalloproteinases have been identified along with some specific tissue inhibitors (TIMPS).
The sharp denaturation temperature of collagen attests to the almost crystalline character of the triple helix and the variation in shrinkage temperature between species is primarily due to the number of hydroxyproline based water hydrogen bridges. The presence of a hydroxyproline deficient thermally labile domain near the carboxy terminus of the molecule initiates the melting process allowing the triple helix to unzip along its length.
Recent studies have demonstrated that collagen is not an inert structural material but interacts with other molecules to control the development of collagenous tissues. Despite the ancient lineage of this ubiquitous protein, collagen is still revealing exciting new scientific features.Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=7903
in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC) > Vol. 82, N° 3 (05-06/1998) . - p. 104-110[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 007022 - Périodique Bibliothèque principale Documentaires Disponible Collagen-PEO composite nanofibers by electrospinning / Zhao Zinzhe in CHEMICAL FIBERS INTERNATIONAL, Vol. 65, N° 1 (03/2015)
[article]
Titre : Collagen-PEO composite nanofibers by electrospinning Type de document : texte imprimé Auteurs : Zhao Zinzhe, Auteur ; Gao Jing, Auteur ; Wang Lu, Auteur ; Wang Fujun, Auteur ; Wang Wenbin, Auteur Année de publication : 2015 Article en page(s) : p. 50-51 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Caractérisation
Collagène
Conduction électrique
Electrofilature
Fourier, Spectroscopie infrarouge à transformée de
Morphologie (matériaux)
Nanofibres
Nontissés
Polyéthylène glycol
ViscositéIndex. décimale : 677.4 Textiles artificiels Résumé : Collagen-polyethylene oxide (PEO) complex nanofibers were prepared by dissolving type 1 collagen in a mixture of HFIP and acetic acid (50:50, vlv). The weight ratios of collagen to PEO were set at 90:10, 80:20 and 70:30. Influences of viscosity and electrical conductivity on the morphology of elec¬trospun nanofibers were investigated. It was proved that nanofibers became finer and finer with the ratio of PEO content increasing. Molecular interac¬tions in collagen-PEO complex and triple helix structure of collagen were also characterized by Fourier transform infrared spectroscopy (FT-IR). lt was found that the triple helix structures of collagen were well preserved in the nanowoven matrix and there were strong hydrogen bonds between PEO and collagen. Note de contenu : - Preparation of the electrospun
- Electrospinning
- Cross-linking
- Characterizations of morphology and chemical structures of the nanofibersEn ligne : https://drive.google.com/file/d/1h-nA2kwY5umsURjjyHP7AjSS0Ou1Je4L/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=23680
in CHEMICAL FIBERS INTERNATIONAL > Vol. 65, N° 1 (03/2015) . - p. 50-51[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 17120 - Périodique Bibliothèque principale Documentaires Disponible Collagen's new age : fColI(h), a wild plant-based fragment of collagen I / Ma Neus Fullana in SOFW JOURNAL, Vol. 148, N° 6 (06/2022)
[article]
Titre : Collagen's new age : fColI(h), a wild plant-based fragment of collagen I Type de document : texte imprimé Auteurs : Ma Neus Fullana, Auteur ; Miriam Mateu, Auteur ; Ariadna Grau-Campistany, Auteur ; Silvia Pastor, Auteur ; Isabel Bronchalo, Auteur Année de publication : 2022 Article en page(s) : 26-31 Note générale : Bibliogr. Langues : Anglais (eng) Catégories : Antiâge
Cellules -- Adhésivité
Collagène
Dermo-cosmétologie
Evaluation
Intégrine
Peau -- Soins et hygiène
Régénération (biologie)Index. décimale : 668.5 Parfums et cosmétiques Résumé : The cosmetic industry is continuously seeking for innovative and reliable products. For generations, collagen has become one of the most trustworthy ingredients due to its efficacy and its interesting properties: anti-aging, moisturizer, humectant, among others. Substantiated concerns have been raised with regard to quality, safety and consistency of animal-sourced collagen. In this context, it has been developed a plant-based fragment of human type I collagen, which is of high purity and contains the proper post-translational modifications to be completely functional due to the use of wild-plant as biofactories’ technology. This identical-to-human fragment collagen type I has been shown to have broad efficacy in and tests, as well as a potent anti-aging effect in clinical studies. These interesting properties highlights fColI(h) as a highly effective and safer source of collagen in the very near future. Note de contenu : - MATERIALS AND METHODS : Epidermal adhesion - Procollagen type I modulation - Collagen-binding integrin expression - Collagen-matrix contraction assay - Skin renewal - Senescence protection - Anti-aging clinical evaluation
- RESULTS AND DISCUSSION : Epidermal adhesion - Surface tensor effect - Procollagen type I modulation - Collagen-binding integrin expression - Collagen-matrix contraction assay - Skin renewal - Senescence protection - Anti-aging clinical evaluationEn ligne : https://drive.google.com/file/d/1Bm5Roviz0XsnFKaKtx8a00azGK2BK4Eq/view?usp=drive [...] Format de la ressource électronique : Permalink : https://e-campus.itech.fr/pmb/opac_css/index.php?lvl=notice_display&id=37816
in SOFW JOURNAL > Vol. 148, N° 6 (06/2022) . - 26-31[article]Réservation
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Code-barres Cote Support Localisation Section Disponibilité 23477 - Périodique Bibliothèque principale Documentaires Disponible Collagen D-spacing and the effect of fat liquor addition / Katie H. Sizeland in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CX, N° 3 (03/2015)
PermalinkLe collagène n'a pas fini de surprendre / Rachida Nachat-Kappes in EXPRESSION COSMETIQUE, N° 64 (07-08/2020)
PermalinkCombattre les rides : rêve ou réalité ? / Jean-Claude Le Joliff in L'ACTUALITE CHIMIQUE, N° 299 (07/2006)
PermalinkComparative analysis of the proteomic profile of cattle hides that produce loose and tight leather using in-gel tryptic digestion followed by LC-MS/MS / Catherine Maidment in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXV, N° 11 (11/2020)
PermalinkA comparative study of various collagen fibre waste as oil sorbent materials / Weining Du in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 99, N° 6 (11-12/2015)
PermalinkPermalinkConnective tissue response to fractionated thermo-ablative erbium / M. O. Bodendorf in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 32, N° 6 (12/2010)
PermalinkConséquences de la glycation in vitro sur le collagène fibreux de type I / Mickaël Meli / 2000
PermalinkContribution à l'étude des complexes Cr3+ - acide polyacrylique et du système Cr3+ - acide polyacrylique-collagène / Abdessatar Toumi / 1984
PermalinkContribution à l'étude viscométrique en solutions diluées de collagène acido-soluble d'origine bovine / Jean-Claude Ronzon / 1987
PermalinkCross-linking phosphoric acid hydrolysates of collagen with cyanidric chloride / I. Chakarska in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 92, N° 2 (03-04/2008)
PermalinkA dehydration process for ovine hide to obtain a new collagenous material / Lluis Ollé in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 98, N° 2 (03-04/2014)
PermalinkDer kollagenreport in INDUSTRIE DU CUIR (IDC), N° 2008/05 (10-11/2008)
PermalinkDesign of a prototype to produce a new collagen material by dehydration / Lluis Ollé in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 97, N° 6 (11-12/2013)
PermalinkDevelopment and characterization of genipin cross-linked gelatin based composites incorporated with vegetable-tanned collagen fiber (VCF) / Jie Liu in JOURNAL OF THE AMERICAN LEATHER CHEMISTS ASSOCIATION (JALCA), Vol. CXII, N° 12 (12/2017)
PermalinkDevelopment of an in vitro model of menopause using primary human dermal fibroblasts / Noëlle Remoué in INTERNATIONAL JOURNAL OF COSMETIC SCIENCE, Vol. 35, N° 6 (12/2013)
PermalinkDifferences in the reaction of condensed and hydrolysable tannins with collagen / Karl Helmer Gustavson in JOURNAL OF THE SOCIETY OF LEATHER TRADES' CHEMISTS, Vol. 50, N° 12 (12/1966)
PermalinkLa diffraction des rayons X et la spectrophotométrie IR : Meilleure connaissance de la structure du collagène, afin d'améliorer la qualité du cuir / A. Huc in TECHNICUIR, N° 7 (08-09/1973)
PermalinkDissolution characteristics of protein in an ionic liquid / Xia Chunchun in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 97, N° 1 (01-02/2013)
PermalinkDynamic mechanical thermal analysis (DMTA) of leather. Part 1 : Effect of tanning agent on the glass transition temperature of collagen / S. Jeyapalina in JOURNAL OF THE SOCIETY OF LEATHER TECHNOLOGISTS & CHEMISTS (JSLTC), Vol. 91, N° 6 (11-12/2007)
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