| Aggregation and self assembly of non-enzymatic glycation of collagen in the presence of amino guanidine and aspirin: an in vitro study. | |
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MedLine Citation:
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PMID: 20600266 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Non-enzymatic glycation of collagen has been used in modern biomaterials science. This paper deals with in vitro studies on the effects of amino guanidine (AG) and aspirin in the non-enzymatic glycation (NEG) of collagen using thermal, conformational, fluorescence, turbidity and powder XRD measurements. There is no significant change in the fluorescence emission spectra for different concentrations of AG treated NEG of collagen whereas the emission intensity decreases as the concentration of aspirin increases. Circular dichroism (CD) revealed the disappearance of the positive peak at 220nm for glycated collagen in the presence of amino guanidine and aspirin suggesting the collapse of triple helical configuration. Nearly 15 degrees C decrease is observed in shrinkage temperature of glycated rat tail tendon (RTT) collagen fibres in the presence of aspirin. Powder XRD of glycated collagen nano-fibrils in the presence of amino guanidine reveals high crystalline nature and the enhancement of self assembly processes when compared to aspirin. To the best of our knowledge, this is the first report of powder XRD of the self assembly of collagen nano-fibrils without mineralization. Our experimental results suggest that in the non-enzymatic glycation of collagen both AG and aspirin play a pivotal role in the aggregation and self assembly processes. From the present study, it is possible to conclude that while AG significantly influences the self assembly processes, aspirin facilitates the aggregation processes. |
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Authors:
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R Usha; S M Jaimohan; A Rajaram; A B Mandal |
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Publication Detail:
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Type: Journal Article Date: 2010-07-01 |
Journal Detail:
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Title: International journal of biological macromolecules Volume: 47 ISSN: 1879-0003 ISO Abbreviation: Int. J. Biol. Macromol. Publication Date: 2010 Oct |
Date Detail:
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Created Date: 2010-08-06 Completed Date: 2011-01-10 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7909578 Medline TA: Int J Biol Macromol Country: Netherlands |
Other Details:
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Languages: eng Pagination: 402-9 Citation Subset: IM |
Affiliation:
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Biophysics Laboratory, Central Leather Research Institute, Council of Scientific and Industrial Research, Adyar, Chennai, India. usharamamoorthy54@yahoo.co.in |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Absorption Animals Aspirin / pharmacology* Calorimetry, Differential Scanning Circular Dichroism Collagen / chemistry, metabolism* Glycosylation / drug effects Guanidines / pharmacology* Nephelometry and Turbidimetry Protein Conformation Rats Spectrometry, Fluorescence Temperature Viscosity X-Ray Diffraction |
| Chemical | |
Reg. No./Substance:
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0/Guanidines; 50-78-2/Aspirin; 79-17-4/pimagedine; 9007-34-5/Collagen |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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