Unveiling the pH dependent interaction between bolaamphiphiles (dicarboxylic acids) and C10TAB (decyltrimethylammonium bromide) in aqueous medium

2018 ◽  
Vol 518 ◽  
pp. 225-233 ◽  
Author(s):  
Animesh Pan ◽  
Subhash C. Bhattacharya ◽  
Animesh K. Rakshit ◽  
Satya P. Moulik
2009 ◽  
Vol 85 (2) ◽  
pp. 463-470 ◽  
Author(s):  
Kalyan C. Tirupula ◽  
Fernanda Balem ◽  
Naveena Yanamala ◽  
Judith Klein-Seetharaman

Langmuir ◽  
2014 ◽  
Vol 30 (6) ◽  
pp. 1588-1598 ◽  
Author(s):  
Sugam Kumar ◽  
Vinod K. Aswal ◽  
P. Callow

2013 ◽  
Vol 5 (S1) ◽  
Author(s):  
Kai Stueckenschneider ◽  
Juliane Merz ◽  
Victor Milman ◽  
Gerhard Schembecker

2014 ◽  
Vol 16 (31) ◽  
pp. 16547-16562 ◽  
Author(s):  
M. Micaela Gonzalez ◽  
M. Paula Denofrio ◽  
Fernando S. García Einschlag ◽  
Carlos A. Franca ◽  
Reinaldo Pis Diez ◽  
...  

The nature of nucleotide and the pH modulate the type of complexes formed and the dynamic deactivation processes.


2016 ◽  
Vol 18 (47) ◽  
pp. 32266-32271 ◽  
Author(s):  
Bo Yu ◽  
Yunyun Huang ◽  
Jun Zhou ◽  
Tuan Guo ◽  
Bai-Ou Guan

A method based on a fiber-optic interferometer to study the pH-dependent interaction between graphene oxide and single-stranded DNA chains is carried out.


2007 ◽  
Vol 126 (2) ◽  
pp. 764-770 ◽  
Author(s):  
Anindita Chatterjee ◽  
Amiya Priyam ◽  
Subhash C. Bhattacharya ◽  
Abhijit Saha

2002 ◽  
Vol 50 (2) ◽  
pp. 327-331 ◽  
Author(s):  
Radhia Mahfoud ◽  
Marc Maresca ◽  
Maurice Santelli ◽  
Annie Pfohl-Leszkowicz ◽  
Antoine Puigserver ◽  
...  

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Sofia Unnerståle ◽  
Lena Mäler

C-peptide is the connecting peptide between the A and B chains of insulin in proinsulin. In this paper, we investigate the interaction between C-peptide and phospholipid bicelles, by circular dichroism and nuclear magnetic resonance spectroscopy, and in particular the pH dependence of this interaction. The results demonstrate that C-peptide is largely unstructured independent of pH, but that a weak structural induction towards a short stretch of β-sheet is induced at low pH, corresponding to the isoelectric point of the peptide. Furthermore, it is demonstrated that C-peptide associates with neutral phospholipid bicelles as well as acidic phospholipid bicelles at this low pH. C-peptide does not undergo a large structural rearrangement as a consequence of lipid interaction, which indicates that the folding and binding are uncoupled. In vivo, local variations in environment, including pH, may cause C-peptide to associate with lipids, which may affect the aggregation state of the peptide.


FEBS Letters ◽  
2007 ◽  
Vol 582 (2) ◽  
pp. 215-220 ◽  
Author(s):  
Francesca Re ◽  
Silvia Sesana ◽  
Alberto Barbiroli ◽  
Francesco Bonomi ◽  
Emanuela Cazzaniga ◽  
...  

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