Next Article in Journal
Phenolic Constituents, Antioxidant and Preliminary Antimycoplasmic Activities of Leaf Skin and Flowers of Aloe vera (L.) Burm. f. (syn. A. barbadensis Mill.) from the Canary Islands (Spain)
Next Article in Special Issue
Application of Reductive 13C-Methylation of Lysines to Enhance the Sensitivity of Conventional NMR Methods
Previous Article in Journal
A Preliminary Study of the Effect of DBD Plasma and Osmolytes on T98G Brain Cancer and HEK Non-Malignant Cells
Molecules 2013, 18(5), 4929-4941; doi:10.3390/molecules18054929
Article

Structural Characterization by NMR of a Double Phosphorylated Chimeric Peptide Vaccine for Treatment of Alzheimer’s Disease

1,* , 2
, 3
, 2
 and 1
Received: 7 February 2013; in revised form: 19 April 2013 / Accepted: 22 April 2013 / Published: 26 April 2013
(This article belongs to the Special Issue NMR of Proteins and Small Biomolecules)
Download PDF [422 KB, uploaded 18 June 2014]
Abstract: Rational design of peptide vaccines becomes important for the treatment of some diseases such as Alzheimer’s disease (AD) and related disorders. In this study, as part of a larger effort to explore correlations of structure and activity, we attempt to characterize the doubly phosphorylated chimeric peptide vaccine targeting a hyperphosphorylated epitope of the Tau protein. The 28-mer linear chimeric peptide consists of the double phosphorylated B cell epitope Tau229-237[pThr231/pSer235] and the immunomodulatory T cell epitope Ag85B241-255 originating from the well-known antigen Ag85B of the Mycobacterium tuberculosis, linked by a four amino acid sequence -GPSL-. NMR chemical shift analysis of our construct demonstrated that the synthesized peptide is essentially unfolded with a tendency to form a β-turn due to the linker. In conclusion, the -GPSL- unit presumably connects the two parts of the vaccine without transferring any structural information from one part to the other. Therefore, the double phosphorylated epitope of the Tau peptide is flexible and accessible.
Keywords: NMR spectroscopy; Biological Magnetic Resonance Data Bank; Alzheimer’s disease; peptide vaccine; B cell epitope; T cell epitope; Tau protein; hyperphosphorylation; Mycobacterium tuberculosis NMR spectroscopy; Biological Magnetic Resonance Data Bank; Alzheimer’s disease; peptide vaccine; B cell epitope; T cell epitope; Tau protein; hyperphosphorylation; Mycobacterium tuberculosis
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Export to BibTeX |
EndNote


MDPI and ACS Style

Ramírez-Gualito, K.; Richter, M.; Matzapetakis, M.; Singer, D.; Berger, S. Structural Characterization by NMR of a Double Phosphorylated Chimeric Peptide Vaccine for Treatment of Alzheimer’s Disease. Molecules 2013, 18, 4929-4941.

AMA Style

Ramírez-Gualito K, Richter M, Matzapetakis M, Singer D, Berger S. Structural Characterization by NMR of a Double Phosphorylated Chimeric Peptide Vaccine for Treatment of Alzheimer’s Disease. Molecules. 2013; 18(5):4929-4941.

Chicago/Turabian Style

Ramírez-Gualito, Karla; Richter, Monique; Matzapetakis, Manolis; Singer, David; Berger, Stefan. 2013. "Structural Characterization by NMR of a Double Phosphorylated Chimeric Peptide Vaccine for Treatment of Alzheimer’s Disease." Molecules 18, no. 5: 4929-4941.


Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert