Related ArticlesSpectroscopic characterization of nanoErythrosomes in the absence and presence of conjugated polyethyleneglycols: an FTIR and (31)P-NMR study.
Biochim Biophys Acta. 2002 Aug 31;1564(2):317-24
Authors: Pouliot R, Saint-Laurent A, Chypre C, Audet R, Vitté-Mony I, -Gaudreault RC, Auger M
We have recently developed from red blood cells a new delivery system called nanoErythrosomes. These nanovesicles offer a high degree of versatility for the encapsulation of biological or nonbiological compounds and for the binding of targeting agents. In particular, polyethyleneglycols can be conjugated by a covalent link to the basic amino acid residues constitutive of the different proteins. The binding of polyethyleneglycols to the nanoErythrosome membrane could be interesting for the therapeutic use of this delivery system since it could overcome heterologous immunogenicity and reduce rapid clearance from circulation. In the present study, we have investigated the effect of temperature on the nanoErythrosome behavior in the absence and presence of conjugated polyethyleneglycols. More specifically, Fourier transform infrared (FTIR) spectroscopy has been used to evaluate the lipid order and dynamics, the hydration and the degree of protein aggregation of the nanoErythrosomes after covalent binding of polyethyleneglycols having molecular weights of 2000 and 5000 g mol(-1). The results indicate that the nanoErythrosome lipid chain order is not significantly affected by heating the nanoErythrosomes at temperatures up to 50 degrees C. They also indicate that the nanoErythrosome proteins aggregate irreversibly at temperatures above 37 degrees C, this effect being abolished in the presence of polyethyleneglycols. The presence of polyethyleneglycols decreases the accessibility of water to the lipid head groups. On the other hand, 31P-nuclear magnetic resonance (NMR) and electron microscopy results reveal that the presence of polyethyleneglycols prevents the aggregation of the nanoErythrosome structures.
More AccurateJCHCoupling Measurement in the Presence ofJHHStrong Coupling in Natural Abundance
More AccurateJCHCoupling Measurement in the Presence ofJHHStrong Coupling in Natural Abundance
Publication year: 2011
Source: Journal of Magnetic Resonance, Available online 22 September 2011</br>
Bingwu*Yu, Hugo*van Ingen, Subramanian*Vivekanandan, Christoph*Rademacher, Scott E.*Norris, ...</br>
Jcouplings are essential for measuring RDCs (residual dipolar couplings), now routinely used to deduce molecular structure and dynamics of glycans and proteins. Accurate measurement ofJCHis critical for RDCs to reflect the true structure and dynamics in the molecule of interest. We report...
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09-24-2011 06:04 AM
[Question from NMRWiki Q&A forum] Can correct TAUc be a sufficient evidence of the absence of aggregation?
Can correct TAUc be a sufficient evidence of the absence of aggregation?
Hello!
I am studying the protein backbone dynamics using the standard set of NMR relaxation parameters (R1, R2, NOE). I would like to be sure that there is no aggregation in the sample, and I have doubts about it so far. The best evidence I have is that overall rotational correlation time TAUc, predicted by HYDRONMR, matches exactly the one calculated from averaged R2/R1 values. Can anyone tell me for sure it is enough and I can be sure that protein doesn't form dimers/oligomers?
Thanks!
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06-10-2011 01:50 PM
[NMR paper] NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements.
NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements.
Related Articles NMR spectroscopic characterization of millisecond protein folding by transverse relaxation dispersion measurements.
J Am Chem Soc. 2005 Sep 28;127(38):13207-12
Authors: Zeeb M, Balbach J
The cold shock protein CspB adopts its native and functional tertiary structure on the millisecond time scale. We employed transverse relaxation NMR methods, which allow a quantitative measurement of the cooperativity of this...
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12-01-2010 06:56 PM
[NMR paper] NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.
NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.
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Biochemistry. 2001 May 8;40(18):5414-21
Authors: MacRaild CA, Hatters DM, Howlett GJ, Gooley PR
The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to (15)N-labeled protein. Micellar SDS, a commonly used...
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11-19-2010 08:32 PM
[NMR paper] Absence of observable biotin-protein interactions in the 1.3S subunit of transcarboxy
Absence of observable biotin-protein interactions in the 1.3S subunit of transcarboxylase: an NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Absence of observable biotin-protein interactions in the 1.3S subunit of transcarboxylase: an NMR study.
Biochemistry. 1997 Dec 2;36(48):14676-82
Authors: Reddy DV, Shenoy BC, Carey PR, Sönnichsen FD
Transcarboxylase (TC) is a biotin-containing enzyme catalyzing the transfer of a carboxyl group from methylmalonyl-CoA to pyruvate to form...
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08-22-2010 05:08 PM
[NMR paper] Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deute
Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS.
Related Articles Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS.
J Biomol NMR. 1993 Jan;3(1):121-6
Authors: Anglister J, Grzesiek S, Ren H, Klee CB, Bax A
At the concentration needed for NMR, the calcium-saturated form of calcineurin B dissolved in water shows resonance line widths that indicate aggregation of this protein. Although the line width or aggregation state can be...
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08-21-2010 11:53 PM
[NMR paper] Spectroscopic characterization of polyethyleneglycol modified superoxide dismutase: 1
Spectroscopic characterization of polyethyleneglycol modified superoxide dismutase: 1H NMR studies on its Cu2Co2 derivative.
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J Inorg Biochem. 1990 Jun;39(2):149-59
Authors: Banci L, Bertini I, Caliceti P, Monsù Scolaro L, Schiavon O, Veronese FM
Spectroscopic methods have been employed in order to understand the molecular basis of the decrease in enzymatic activity of the antiinflammatory enzyme...
Spectroscopic characterization of nanoErythrosomes in the absence and presence of con
Linear Mode
