Study on peptide-peptide interactions between transmembrane domains of Slc11a1 in model membranes

Haiyan Qi; Xiuwen Wang; Liqiang Su; Shu Wang; Ying Wang

doi:10.1016/j.saa.2021.119594

Study on peptide-peptide interactions between transmembrane domains of Slc11a1 in model membranes

Spectrochim Acta A Mol Biomol Spectrosc. 2021 May 15:253:119594. doi: 10.1016/j.saa.2021.119594. Epub 2021 Feb 19.

Authors

Haiyan Qi¹, Xiuwen Wang², Liqiang Su², Shu Wang², Ying Wang²

Affiliations

¹ College of Chemistry and Chemical Engineering, Qiqihar University, No. 42, Wenhua Street, Qiqihar, PR China; Heilongjiang Industrial Hemp Processing Technology Innovation Center, PR China. Electronic address: qhy120@sina.com.
² College of Chemistry and Chemical Engineering, Qiqihar University, No. 42, Wenhua Street, Qiqihar, PR China.

PMID: 33662699
DOI: 10.1016/j.saa.2021.119594

Abstract

In this study, we determined the interaction between TM4 and TM2/TM3 domain of Solute carrier family 11 member 1 (Slc11a1) by circular dichroism (CD) and fluorescence spectrum. The results indicated that, the cation transport process was likely to be accomplished by the collaboration of multiple TM domains rather than by TM4 domain alone. Therefore, this finding suggested possible transportation theory and be helpful to elucidate the mechanism of Slc11a1 in cation transport process.

Keywords: Interaction; Slc11a1; Spectroscopy; Transmembrane domains.

MeSH terms

Circular Dichroism
Peptides*

Substances

Peptides