期刊
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
卷 102, 期 -, 页码 186-193出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2012.10.048
关键词
Collagen; Intrinsic fluorescence; Two-phase diagram; Two-dimensional correlation map; Aggregation
类别
资金
- National Nature Science Foundation of China [21076129/B060805]
The aggregation behavior of type I collagen in acid solutions with the concentrations covering a range of 0.06-1.50 mg/mL was studied utilizing both of the fluorescence resonance energy transfer (FRET) between the phenylalanine and tyrosine residues and the external probing of 1,8-anilinonaphthalene sulfonate (ANS). FRET at 0.30 mg/mL showed the distance among collagen monomers was within 10 nm without the obvious aggregates formed. The predominance of tyrosine fluorescence in FRET in the range of 0.45-0.75 mg/mL identified the existence of collagen aggregates companied with the formation of hydrophobic microdomains revealed by the change of the fluorescence of ANS. The blue-shift of tyrosine fluorescence from 303 to 293 nm for 0.90-1.50 mg/mL dedicated the formation of high order aggregates. The results from the two-phase diagrams of the intrinsic fluorescence for the guanidine hydrochloride-induced unfolding of collagen confirmed these conclusions. By the two-dimensional correlation analysis for the intrinsic fluorescence of collagen solutions of 0.45, 0.75 and 1.05 mg/mL, the probable characteristic fluorescence peaks for the interactions of proline-aromatic (CH similar to pi) among the collagen molecules were found at 298 and 316 nm. (C) 2012 Elsevier B.V. All rights reserved.
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