8H0U

AQEE-30 in a DPC solution

Summary for 8H0U

• Entry DOI: 10.2210/pdb8h0u/pdb
• Descriptor: AQEE-30 (1 entity in total)
• Functional Keywords: vgf, dpc, neuropeptide
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 3800.08

Authors

Park, O.-S.,Jeon, Y.H.,Cheong, C. (deposition date: 2022-09-30, release date: 2022-12-14, Last modification date: 2024-05-15)

Primary citation

Park, O.S.,Bang, J.K.,Cheong, C.,Jeon, Y.H.
Structure of AQEE-30 of VGF Neuropeptide in Membrane-Mimicking Environments.
Int J Mol Sci, 23:-, 2022

PubMed Abstract: AQEE-30 is one of the VGF peptides, which are derived from the VGF polypeptide precursor, and related to various physiological phenomena including neuroprotective effects in Huntington's disease and amyotrophic lateral sclerosis (ALS). Although various functions of AQEE-30 have been reported so far, the structure of this peptide has not been reported yet. In this study, the structure of human AQEE-30 was investigated in hexafluoroisopropanol (HFIP) and dodecyl phosphocholine (DPC) micelle solutions, using circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy. CD results showed that AQEE-30 had a partial helical structure in aqueous buffer, and the helical structure was stabilized in the HFIP and DPC micelle solutions. The 3D structures determined by NMR spectroscopy showed that AQEE-30 adopted mainly α-helical structure in both the HFIP and DPC micelle solutions. The surface of AQEE-30 showed that it was predominantly negatively charged. The residues from 601 to 611 in both the HFIP and DPC micelle solutions showed amphiphilicity with four negatively charged residues, glutamate. The C-terminal consecutive arginine residues formed a partial positively charged surface. These results suggest an α-helical active structure of AQEE-30 in the cell-membrane environment.

PubMed: 36430431
DOI: 10.3390/ijms232213953

Experimental method

SOLUTION NMR