Literature DB >> 34855073

Effect of pH on the Conformational Transition of Silk Fibroin in Aqueous Solution Monitored by Thioflavin-T Fluorescence.

Ben Jia1, Lan Jia2, Jingxin Zhu1.   

Abstract

In this work, the potential application of the fluorescence dye Thioflavin-T (ThT), which can specifically bind to amyloid, as a powerful tool for monitoring secondary structural transitions of silk fibroin (SF) induced by pH in low solution concentrations was examined. Results showed that ThT emission intensities substantially increased when pH decreased from 6.8 to 4.8. This increase may be ascribed to conformational transitions from random coil to β-sheet. The morphology and secondary structure of SF were also investigated via TEM, AFM and circular dichroism spectroscopy. The information obtained herein can be utilized not only for the development of convenient and efficient noninvasive method for monitoring the assembly behavior of SF in aqueous solution but also for in vitro fluorescence imaging.
© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Conformational transition; Fluorescence spectroscopy; Protein structures; Silk fibroin; Thioflavin-T

Mesh:

Substances:

Year:  2021        PMID: 34855073     DOI: 10.1007/s10895-021-02841-x

Source DB:  PubMed          Journal:  J Fluoresc        ISSN: 1053-0509            Impact factor:   2.217


  9 in total

1.  Quantification of beta-sheet amyloid fibril structures with thioflavin T.

Authors:  H LeVine
Journal:  Methods Enzymol       Date:  1999       Impact factor: 1.600

2.  Structural evolution of regenerated silk fibroin under shear: combined wide- and small-angle x-ray scattering experiments using synchrotron radiation.

Authors:  Manfred Rössle; Pierre Panine; Volker S Urban; Christian Riekel
Journal:  Biopolymers       Date:  2004-07       Impact factor: 2.505

3.  Effects of pH and calcium ions on the conformational transitions in silk fibroin using 2D Raman correlation spectroscopy and 13C solid-state NMR.

Authors:  Ping Zhou; Xun Xie; David P Knight; Xiao-Hong Zong; Feng Deng; Wen-Hua Yao
Journal:  Biochemistry       Date:  2004-09-07       Impact factor: 3.162

Review 4.  Probing protein folding and conformational transitions with fluorescence.

Authors:  Catherine A Royer
Journal:  Chem Rev       Date:  2006-05       Impact factor: 60.622

5.  Mechanisms of tryptophan fluorescence shifts in proteins.

Authors:  J T Vivian; P R Callis
Journal:  Biophys J       Date:  2001-05       Impact factor: 4.033

6.  Intrinsic fluorescence changes associated with the conformational state of silk fibroin in biomaterial matrices.

Authors:  Irene Georgakoudi; Irene Tsai; Cherry Greiner; Cheryl Wong; Jordy Defelice; David Kaplan
Journal:  Opt Express       Date:  2007-02-05       Impact factor: 3.894

7.  Residue-Specific Binding Mechanisms of Thioflavin T to a Surface of Flat β-Sheets within a Peptide Self-Assembly Mimic.

Authors:  Sae Namioka; Norio Yoshida; Hiroyuki Konno; Koki Makabe
Journal:  Biochemistry       Date:  2020-06-10       Impact factor: 3.162

8.  Conformation transition kinetics of regenerated Bombyx mori silk fibroin membrane monitored by time-resolved FTIR spectroscopy.

Authors:  X Chen; Z Shao; N S Marinkovic; L M Miller; P Zhou; M R Chance
Journal:  Biophys Chem       Date:  2001-01-31       Impact factor: 2.352

9.  Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status.

Authors:  Minna Groenning
Journal:  J Chem Biol       Date:  2009-08-20
  9 in total

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