Membrane Protein Analyses Using Alkylated Trihydroxyacetophenone (ATHAP) as a MALDI Matrix

Analytical Chemistry
Yuko FukuyamaKoichi Tanaka

Abstract

Membrane proteins containing hydrophobic regions have been difficult to analyze using MALDI-MS, probably due to the use of conventional matrices with a low affinity for hydrophobic peptides. Recently, we reported 1-(2,4,6-trihydroxyphenyl)octan-1-one (alkylated trihydroxyacetophenone (ATHAP)) as a matrix for hydrophobic peptides. In this study, ATHAP was applied to analyze membrane proteins containing transmembrane domains. As a result, we detected intact molecular ions for bacteriorhodopsin (BR) containing seven transmembrane domains that are difficult to detect using 2,4,6-trihydroxyacetophenone or sinapinic acid, by using ATHAP. In addition, we detected digest ions containing all seven transmembrane domains that are difficult to detect using α-cyano-4-hydroxycinnamic acid (CHCA), by using ATHAP. Moreover, ions for hydrophobic digests containing a single transmembrane domain for cadherin 1 (CDH1), fibroblast growth factor receptor 4 (FGFR4), epithelial cell adhesion molecule (EPCAM) recombinant proteins, and human epidermal growth factor receptor type 2 (HER2) were detected with higher sensitivity using ATHAP than with CHCA, confirming that ATHAP improved the membrane protein analyses, especially for hydrophobic regions such ...Continue Reading

References

Apr 2, 1974·Archives of Biochemistry and Biophysics·H B Bull, K Breese
May 6, 1998·Protein Science : a Publication of the Protein Society·E Wallin, G von Heijne
Apr 15, 2003·Nature Biotechnology·Christine C WuJohn R Yates
Oct 9, 2007·Nature Biotechnology·Muhammed A YildirimMarc Vidal
Jan 11, 2008·Journal of Proteome Research·Takeshi MasudaYasushi Ishihama
Dec 18, 2009·Proteomics·Benjamin RietschelBjoern Meyer
Nov 17, 2010·Analytical and Bioanalytical Chemistry·Liangliang SunYukui Zhang
Jun 28, 2011·Electrophoresis·Marijana RucevicDjuro Josic
Apr 18, 2012·Analytical Chemistry·Yuko FukuyamaKoichi Tanaka
Jan 11, 2013·Analytical Chemistry·Julian P Whitelegge
Sep 12, 2013·Molecular & Cellular Proteomics : MCP·Adam D CathermanNeil L Kelleher
Sep 26, 2013·Analytical Chemistry·Yuko FukuyamaKoichi Tanaka
Nov 1, 2013·Molecular & Cellular Proteomics : MCP·Marcella Nunes Melo-BragaMartin Røssel Larsen

❮ Previous
Next ❯

Citations

Aug 14, 2018·Chemical Communications : Chem Comm·Yuning WangBaohong Liu
Jan 21, 2017·Analytical Chemistry·Patricia M PeacockSarah Trimpin

❮ Previous
Next ❯

Related Concepts

Related Feeds

Cadherins and Catenins

Cadherins (named for "calcium-dependent adhesion") are a type of cell adhesion molecule (CAM) that is important in the formation of adherens junctions to bind cells with each other. Catenins are a family of proteins found in complexes with cadherin cell adhesion molecules of animal cells: alpha-catenin can bind to β-catenin and can also bind actin. β-catenin binds the cytoplasmic domain of some cadherins. Discover the latest research on cadherins and catenins here.

Adhesion Molecules in Health and Disease

Cell adhesion molecules are a subset of cell adhesion proteins located on the cell surface involved in binding with other cells or with the extracellular matrix in the process called cell adhesion. In essence, cell adhesion molecules help cells stick to each other and to their surroundings. Cell adhesion is a crucial component in maintaining tissue structure and function. Discover the latest research on adhesion molecule and their role in health and disease here.