Molecular recognition and interaction between human plasminogen Kringle 5 and voltage-dependent anion channel-1 by biological specificity technologies and molecular dynamic simulation

Voltage-dependent anion channel-l (VDAC-1) can bind with plasminogen Kringle 5 as the cell surface receptor and induce cell apoptosis, but the detailed information of binding is not clear yet. Thus, the mutual recognition and binding were investigated here utilizing frontal affinity chromatography,...

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Veröffentlicht in:	Biophysical chemistry 2022-01, Vol.280, p.106710-106710, Article 106710
Hauptverfasser:	Zhang, Jiaxin, Wang, Kun, Xue, Pengli, Chen, Xiu, Bian, Liujiao
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites Frontal affinity chromatography Human plasminogen Kringle 5 Humans Molecular Dynamics Simulation Molecular recognition and binding Peptide Fragments Plasminogen Protein Binding Surface plasma resonance Voltage-Dependent Anion Channel 1 - metabolism Voltage-dependent anion channel-1 Voltage-Dependent Anion Channels - metabolism
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