Semidilute solution structure of cellulose in an ionic liquid and its mixture with a polar organic co-solvent studied by small-angle X-ray scattering

2017 ◽  
Vol 55 (11) ◽  
pp. 888-894 ◽  
Author(s):  
Sofia Napso ◽  
Dmitry M. Rein ◽  
Rafail Khalfin ◽  
Yachin Cohen
Keyword(s):  
Ionic Liquid ◽  
Small Angle ◽  
Solution Structure ◽  
X Ray ◽  
X Ray Scattering ◽  
Semidilute Solution ◽  
Ray Scattering

scholarly journals A model of the solution structure of human Pex5p obtained by small angle X-ray scattering

2006 ◽  
Vol 62 (a1) ◽  
pp. s264-s264
Author(s):  
K. Shiozawa ◽  
P. Konarev ◽  
C. Neufeld ◽  
W. A. Stanley ◽  
M. Wilmanns ◽  
...  
Keyword(s):  
Small Angle ◽  
Solution Structure ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

Solution Structure of Myosin-ADP-MgFn Ternary Complex by Fluorescent Probes and Small-Angle Synchrotron X-Ray Scattering

2000 ◽  
Vol 128 (4) ◽  
pp. 687-694 ◽  
Author(s):  
S. Manita ◽  
T. Aihara ◽  
Y. Uyehara ◽  
K. Homma ◽  
Y. Sugimoto ◽  
...  
Keyword(s):  
Fluorescent Probes ◽  
Small Angle ◽  
Solution Structure ◽  
Ternary Complex ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals The solution structure and activation of visual arrestin studied by small-angle X-ray scattering

2002 ◽  
Vol 269 (15) ◽  
pp. 3801-3809 ◽  
Author(s):  
Brian H. Shilton ◽  
J. Hugh McDowell ◽  
W. Clay Smith ◽  
Paul A. Hargrave
Keyword(s):  
Small Angle ◽  
Solution Structure ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals Influence of the Cosolute Environment on IgG Solution Structure Analyzed by Small-Angle X-ray Scattering

2012 ◽  
Vol 116 (32) ◽  
pp. 9611-9618 ◽  
Author(s):  
Wayne G. Lilyestrom ◽  
Steven J. Shire ◽  
Thomas M. Scherer
Keyword(s):  
Small Angle ◽  
Solution Structure ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

Solution Structure of C-Terminal Escherichia coli Translation Initiation Factor IF2 by Small-Angle X-ray Scattering†

Biochemistry ◽  
2008 ◽  
Vol 47 (20) ◽  
pp. 5590-5598 ◽  
Author(s):  
Louise Carøe Vohlander Rasmussen ◽  
Cristiano Luis Pinto Oliveira ◽  
Janni Mosgaard Jensen ◽  
Jan Skov Pedersen ◽  
Hans Uffe Sperling-Petersen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Translation Initiation ◽  
Small Angle ◽  
Solution Structure ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals Nano-Structural Investigation on Cellulose Highly Dissolved in Ionic Liquid: A Small Angle X-ray Scattering Study

Molecules ◽  
2017 ◽  
Vol 22 (1) ◽  
pp. 178 ◽  
Author(s):  
Takatsugu Endo ◽  
Shota Hosomi ◽  
Shunsuke Fujii ◽  
Kazuaki Ninomiya ◽  
Kenji Takahashi
Keyword(s):  
Ionic Liquid ◽  
Small Angle ◽  
Structural Investigation ◽  
X Ray ◽  
X Ray Scattering ◽  
Scattering Study ◽  
Ray Scattering

scholarly journals Structure-Activity Study of an All-d Antimicrobial Octapeptide D2D

Molecules ◽  
2019 ◽  
Vol 24 (24) ◽  
pp. 4571
Author(s):  
Abdullah Lone ◽  
Thomas T. Thomsen ◽  
Josefine Eilsø Nielsen ◽  
Peter W. Thulstrup ◽  
Rasmus N. Klitgaard ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Small Angle ◽  
Solution Structure ◽  
Resistant Bacteria ◽  
Dependent Manner ◽  
Structure Model ◽  
X Ray ◽  
X Ray Scattering ◽  
Structure Activity ◽  
Ray Scattering

The increasing emergence of multi-drug resistant bacteria is a serious threat to public health worldwide. Antimicrobial peptides have attracted attention as potential antibiotics since they are present in all multicellular organisms and act as a first line of defence against invading pathogens. We have previously identified a small all-d antimicrobial octapeptide amide kk(1-nal)fk(1-nal)k(nle)-NH2 (D2D) with promising antimicrobial activity. In this work, we have performed a structure-activity relationship study of D2D based on 36 analogues aimed at discovering which elements are important for antimicrobial activity and toxicity. These modifications include an alanine scan, probing variation of hydrophobicity at lys5 and lys7, manipulation of amphipathicity, N-and C-termini deletions and lys-arg substitutions. We found that the hydrophobic residues in position 3 (1-nal), 4 (phe), 6 (1-nal) and 8 (nle) are important for antimicrobial activity and to a lesser extent cationic lysine residues in position 1, 2, 5 and 7. Our best analogue 5, showed MICs of 4 µg/mL against A. baumannii, E. coli, P. aeruginosa and S. aureus with a hemolytic activity of 47% against red blood cells. Furthermore, compound 5 kills bacteria in a concentration-dependent manner as shown by time-kill kinetics. Circular dichroism (CD) spectra of D2D and compounds 1–8 showed that they likely fold into α-helical secondary structure. Small angle x-ray scattering (SAXS) experiments showed that a random unstructured polymer-like chains model could explain D2D and compounds 1, 3, 4, 6 and 8. Solution structure of compound 5 can be described with a nanotube structure model, compound 7 can be described with a filament-like structure model, while compound 2 can be described with both models. Lipid interaction probed by small angle X-ray scattering (SAXS) showed that a higher amount of compound 5 (~50–60%) inserts into the bilayer compared to D2D (~30–50%). D2D still remains the lead compound, however compound 5 is an interesting antimicrobial peptide for further investigations due to its nanotube structure and minor improvement to antimicrobial activity compared to D2D.

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